ライフサイエンスコーパス: papain

1 o other related cysteine proteases (SpeB and papain).

2 and internalization of the cysteine protease papain.

3 for B cells to rapidly bind and internalize papain.

4 monstrate retrieval of the cysteine protease papain.

5 he S2 pocket, which is more spacious than in papain.

6 ngth Cal1 with the general cysteine protease papain.

7 inhibitors of IdeS inhibit neither SpeB nor papain.

8 but also weakly blocks the cysteine protease papain.

9 to prototypic proteases, namely, trypsin and papain.

10 -RAM support before and after treatment with papain.

11 iocarbazate with key active site residues in papain.

12 e result seen for the equivalent mutation in papain.

13 lisin A, trypsin, chymotrypsin, thrombin, or papain.

14 activity to inhibit cathepsins K, B, L, and papain.

15 ns) upon the immunization with ovalbumin and papain.

16 r-Phe-EDANS by the proteases thermolysin and papain.

17 anonical ITAM signaling was not activated by papain.

18 t Th2 cell response to the protease-allergen papain.

19 erential proteolysis profiles of the mAbs by papain.

20 peptidic inhibitors of the cysteine protease papain.

21 n each) but not by chymotrypsin, Pronase, or papain (0.1%, up to 2 min each).

22 Papain, a cysteine protease allergen with inherent adjuv

23 Barrier disruption by papain, a protease with structural homology to Der p 1,

24 pinna, contact sensitization, CpG, LPS, and papain all mobilized DDCs in three distinct phases: incr

25 f target cells with proteases (proteinase K, papain, alpha-chymotrypsin, and trypsin) abrogated entry

26 n induced by two proteases allergens HDM and papain and a classical allergen ovalbumin was evaluated

27 olled and non pH-controlled conditions using papain and a microbial-derived alternative (papain-like

28 Protease preparations from plant (papain and bromelain) and fungal (FP400 and FPII) source

29 ysed using protease preparations from plant (papain and bromelain) and fungal (FP400 and FPII) source

30 ctivities against cysteine proteases such as papain and calpain as well as the human 20S proteasome.

31 nce similarity to cysteine peptidases of the papain and calpain families.

32 ses 1, which inhibits the cysteine proteases papain and cathepsins B, K and L up to 2 times more pote

33 greater selectivity toward cathepsin L than papain and cathepsins B, K, V, and S with no activity ag

34 and disparate to the archetypical proteases papain and chymotrypsin.

35 are equally susceptible to PK and proteases papain and chymotrypsin.

36 Less effective endopin 2C inhibition of papain and elastase occurred with k(ass) association rat

37 ractions of the RSL domain of endopin 2 with papain and elastase were indicated by cleavage of endopi

38 Recombinant N-His-tagged endopin 2 inhibited papain and elastase with second-order rate constants (k(

39 Endopin 2 formed SDS-stable complexes with papain and elastase, a characteristic property of serpin

40 teases, indicated by effective inhibition of papain and elastase, respectively.

41 rity (greater than 80%) to the prodomains of papain and other papain-like enzymes isolated from papay

42 We immunized mice in the footpad with papain and studied leukocyte recruitment and inflammator

43 mined by susceptibility of its C terminus to papain and the endoproteinase, Asp-N, followed by SDS/PA

44 e in reducing gliadin content than the crude papain and the resultant loaves had acceptable crumb and

45 pore size of the support, and the amount of papain and time that were used for support treatment.

46 denatured RBP fractions were hydrolyzed with papain and trypsin for 3h at optimum conditions.

47 At the studied conditions, papain and trypsin were more effective in hydrolyzing Na

48 trypsin, chymotrypsin, pepsin, thermolysin, papain, and calpain.

49 ormed SDS-stable complexes with cathepsin L, papain, and elastase that are typical of serpins.

50 Trypsin, papain, and proteinase K do not cleave band 3 at or near

51 eases such as Pronase, proteinase K, pepsin, papain, and subtilisin.

52 to cysteine proteases, such as bromelain and papain, as a model for allergens.

53 We found that papain at a range of concentrations is nearly as active

54 C) value was obtained for WP hydrolysed with papain at constant pH of 7.0 compared to the associated

55 ble type I collagen membrane were exposed to papain based gel, irradiated with laser and analyzed abo

56 Overall than hydrolysates generated with papain, bromelain and FP400.

57 he range 0.8-3.2mM inhibited the activity of papain, bromelain and zingibain, iso-AA acted as an inhi

58 organic solvents, hot alkali, or proteases (papain, bromelain) diminished the adsorption rates of th

59 AA) on the activity of four plant proteases (papain, bromelain, actinidin and zingibain) and three mi

60 like cysteine proteases (clan CA, family C1) papain, bromelain, and human cathepsins L, V, K, S, F, B

61 different functions, including plant enzymes papain, bromelain, ficin, and mammalian lysosomal cathep

62 preparations from plant and fungal sources (papain, bromelain, FP400 and FPII) were used to hydrolys

63 d zingibain, iso-AA acted as an inhibitor of papain but as an activator of zingibain and had no signi

64 modern cathepsin B, which is a member of the papain (C1) family of cysteine proteinases.

65 acceptors showed no cross reactivity toward papain, cathepsin B, and calpain.

66 vity with clan CA cysteine proteases such as papain, cathepsin B, and calpains.

67 Cruzain is a member of the papain/cathepsin L family of cysteine proteases, and the

68 ; and the cysteine proteases cathepsin B and papain (clan CA), and legumain (clan CD).

69 uncleaved actins protect myosin loop 1 from papain cleavage equally well.

70 ges in near-UV CD spectra, susceptibility to papain cleavage in an adjacent CDR2 loop, and the tenden

71 und in healthy subjects are specific for the papain cleavage site of any Fab fragments and, although

72 or regulator released from the Fc following papain cleavage.

73 In peripheral blood lymphocytes, papain cleaved off HLA class I proteins as effectively a

74 action, affinity purified immunoglobulin, or papain-cleaved antibody fragments had no effect on growt

75 Under conditions when papain could cut both Fab arms of non-nmAbs, only one Fa

76 plication, other eukaryotic PC synthases are papain Cys protease superfamily members but ones, unlike

77 d near that of the extensively characterized papain Cys25.

78 nduced gene silencing (VIGS), that the plant papain cysteine protease cathepsin B is required for the

79 may use a similar catalytic strategy as the papain cysteine proteases, holding its Cys184 side chain

80 Identification and analysis of Clan CA (papain) cysteine proteases in primitive protozoa and met

81 treated and control groups was quantified by papain digest and fluorescence spectrophotometry.

82 ontrol groups was quantified with the use of papain digest and fluorescence spectrophotometry.

83 and small angle x-ray scattering results of papain-digested products revealed that 1) the Fab-Fc or

84 y binds to CD105, was generated by enzymatic papain digestion and conjugated to NOTA (1,4,7-triazacyc

85 trometry-based approach, in combination with papain digestion and partial reduction, to obtain site-s

86 a combination of cation-exchange separation, papain digestion, and a panel of mass spectrometry techn

87 Papain directly activated naive T cells through protease

88 b)-tsA58/+; HRhoGFP/+) or C57BL/6 mice after papain dissociation.

89 Muller cells were isolated from papain-DNase-digested human retina.

90 en bond is absent in nitrile-bound wild-type papain due to the flexibility of the imidazole ring of H

91 family of cysteine proteinases, particularly papain (EC 3.4.22.2) itself, continue to contribute to t

92 Studies on papain (EC 3.4.22.2), the most thoroughly investigated m

93 model applications: (1) characterization of papain enzyme kinetics using rapid-mixing experiments, (

94 in invertebrates, cysteine proteases of the papain family and aspartic proteases assume the role.

95 e have now characterized five genes encoding papain family cathepsins from Toxoplasma gondii, includi

96 Falcipain-2 (FP2) is a papain family cysteine protease and important hemoglobin

97 how that CSP is proteolytically cleaved by a papain family cysteine protease of parasite origin.

98 le is a 262-amino-acid thiol protease of the papain family expressed as a combination of isoforms and

99 nhibitors of human cysteine proteases of the papain family have been made and assayed versus a number

100 Members of the papain family of cysteine cathepsins are among the prote

101 Members of the papain family of cysteine proteases (cathepsins) mediate

102 Although the papain family of cysteine proteases has been considered

103 is contrasts with the evolutionarily related papain family of cysteine proteases, which uses Gln-19 (

104 hanism of human cathepsin K, a member of the papain family of cysteine proteases.

105 racteristically observed with members of the papain family of cysteine proteinases, help to stabilize

106 Studies on members of the papain family of cysteine proteinases, particularly papa

107 ely 130 amino acids is weakly similar to the papain family of proteases and is highly conserved from

108 Unlike other studied papain family proteases, falcipain-2 does not require it

109 e I, is a lysosomal cysteine protease of the papain family that catalyzes the sequential removal of d

110 d to cathepsin K, a cysteine protease of the papain family that is abundantly and selectively express

111 in F is a lysosomal cysteine protease of the papain family, and likely plays a regulatory role in pro

112 ncoding a lysosomal cysteine protease of the papain family, highly up-regulated in the developing lun

113 substrates for cysteine peptidases of the C1 papain family, important in many biological processes.

114 Cysteine proteases of the Clan CA (papain) family are the predominant protease group in pri

115 instead requires the expression of a second papain-family cathepsin protease, TgCPL.

116 udies suggest ideas for inhibitor design for papain-family cysteine proteases and strategies to progr

117 Papain-family cysteine proteases of the malaria parasite

118 his enzyme differs in this regard from other papain-family enzymes.

119 Available data suggest that papain-family proteases require prodomains for correct f

120 red in a circular permutation of the classic papain fold.

121 ly of cysteine proteases, which uses Gln-19 (papain) for stabilizing the transition state.

122 study intended to evaluate the effects of a papain-gel with a red-light absorbing pigment (methylene

123 Papain generated RBCF hydrolysates exhibited higher ferr

124 were similar for the thiolate forms of hAGT, papain, glutathione, and the bacterial hAGT homologue Og

125 onitrile, I) catalyzed by Gln19Glu mutant of papain has been studied by nanosecond molecular dynamics

126 acterized the cellular response activated by papain in basophils.

127 e challenged with house dust mite extract or papain in the absence of TSLPR have a drastic reduction

128 n of eosinophils and heightened responses to papain in the lung and increased ability to expulse the

129 fluenza infection model in mice, and blocked papain-induced acute lung inflammation.

130 otoxin shock, and in the lung alveoli during papain-induced allergic airway inflammation.

131 tion of basophils caused a resolution of the papain-induced eosinophilia and mucus production.

132 principles, was performed in six sheep with papain-induced experimental emphysema (EMPH).

133 We find that papain-induced IL-4 production requires calcium flux and

134 Interestingly, papain-induced IL-4 production was dependent on the immu

135 Papain-induced ILC2 activation and Th2 cell differentiat

136 nd the contribution of various leukocytes to papain-induced immune responses.

137 We found that during papain-induced lung inflammation, IL-9 production was la

138 eas interleukin-4 (IL-4) was dispensable for papain-induced Th2 cell differentiation, ILC2-derived IL

139 We studied how papain induces basophil migration to LNs and the contrib

140 rephthalate (PET), trehalose, and a peptide (papain inhibitor) are enhanced by 35x, 12x, and 3.5x wit

141 o displays specificity: the three identified papain inhibitors did not covalently react with UbcH7, U

142 Papain is a protease with potential use in transplantati

143 In distilled water, papain is as active in cleaving a test substrate at a te

144 This finding also holds true if papain is dissolved in Belzer-UW solution.

145 A cysteine protease, papain, is a prototypic protease allergen that can direc

146 lymerase (RdRp), the self-interaction of the papain like protease, and ORF3 interactions with the pap

147 contains a central domain homologous to the papain-like (clan CA, family C1) protease family.

148 ses: the chymotrypsin-like main protease and papain-like accessory proteases (PLpros).

149 and this part did not exhibit any effect on papain-like activities.

150 WP hydrolysed with papain-like activity under pH regulation at 7.0 displaye

151 papain and a microbial-derived alternative (papain-like activity).

152 a family of calcium-dependent proteases with papain-like activity, the calpains.

153 ribed here reveals that the protein adopts a papain-like alpha+beta fold and identifies a substrate-b

154 fungus Cryphonetria parasitica, encodes two papain-like autocatalytic leader proteases, p29 and p48,

155 Embedded in nsp1beta's papain-like autoproteinase domain, we identified a highl

156 conserved N-terminal domain and a conserved, papain-like C-terminal domain.

157 of TG2 (residues 139-471, rat) comprises the papain-like catalytic triad and the GTP-binding domain (

158 esidues, His-162 and Asp-180 of the putative papain-like catalytic triad of AtPCS1, are essential for

159 7 as a possible third member of the proposed papain-like catalytic triad.

160 ssesses dual specificity for inhibiting both papain-like cysteine and elastase-like serine proteases.

161 s-class inhibitor with activity against both papain-like cysteine and trypsin-like serine proteinases

162 Rcr3 encodes a secreted papain-like cysteine endoprotease.

163 XCP1 is a xylem-specific papain-like cysteine peptidase in Arabidopsis.

164 Cruzipain, the main papain-like cysteine peptidase of T. cruzi, is an import

165 Two domains, X and the papain-like cysteine protease domain (PCP), of HEV ORF1

166 rotease domain, a Ca(2+)- and Zn(2+)-binding papain-like cysteine protease domain within the nonstruc

167 phagoides pteronyssinus, that belongs to the papain-like cysteine protease family.

168 Cathepsin K, a lysosomal papain-like cysteine protease, forms collagenolytically

169 o Rcr3(pim) perturbs the active site of this papain-like cysteine protease.

170 The substrate specificities of papain-like cysteine proteases (clan CA, family C1) papa

171 The primary specificity of papain-like cysteine proteases (family C1, clan CA) is d

172 Papain-like cysteine proteases (PLCPs) are a large class

173 provides an increasing body of evidence for papain-like cysteine proteases (PLCPs) being central hub

174 (GAGs) is unique for cathepsin K among human papain-like cysteine proteases and that different GAGs c

175 and relatively limited number of vertebrate papain-like cysteine proteases during blood feeding.

176 The papain-like cysteine proteases encoded by the coronaviru

177 Cathepsins K and S are papain-like cysteine proteases with known elastolytic ac

178 0, which may be significantly different from papain-like cysteine proteases.

179 The core of this structure resembles the papain-like cysteine proteases.

180 Residue Y283 is highly conserved among papain-like cysteine proteases.

181 tor of both chymotrypsin-like serine and the papain-like cysteine proteinases by employing an RSL-dep

182 ity of serpins to inhibit both serine and/or papain-like cysteine proteinases may not be a recent eve

183 Using an expanded panel of papain-like cysteine proteinases, we now show that SQN-5

184 to inhibit both chymotrypsin-like serine and papain-like cysteine proteinases.

185 is essential in blood stages and possesses a papain-like domain, prompting speculation that it functi

186 n 80%) to the prodomains of papain and other papain-like enzymes isolated from papaya (Carica papaya)

187 of parasitic protozoa belong to the group of papain-like enzymes known as clan CA.

188 cifers when compared with all other reported papain-like enzymes.

189 t EPIC2B interacts with and inhibits a novel papain-like extracellular cysteine protease, termed Phyt

190 Cathepsin W is a member of the papain-like family of cysteine proteases.

191 that the Josephin domain binds Ub and has a papain-like fold that is reminiscent of that of other de

192 structure of SpvD and show that it adopts a papain-like fold with a characteristic cysteine-histidin

193 M48(USP) adopts a papain-like fold, with the active-site cysteine forming

194 frames (ORF), each encoding an autocatalytic papain-like leader protease.

195 ositive-strand RNA viruses encode one or two papain-like leader proteinases.

196 counterparts, which, in addition to having a papain-like N-terminal catalytic domain that undergoes p

197 pressors, comprise a vertebrate subfamily of papain-like or NlpC/P60 thiol proteases that function as

198 Our group reported papain-like properties of beta-expansin of Timothy grass

199 plication depends in part on a virus-encoded papain-like protease (PL(pro)) that cleaves the viral re

200 er of the viral SARS-unique domain (SUD) and papain-like protease (PL(pro)), and, as a consequence, t

201 o 68% amino acid identity to torovirus (ToV) papain-like protease (PLP) (ToV-PLP).

202 identified as interferon (IFN) antagonists, papain-like protease (PLP) and N protein.

203 Structural studies of the papain-like protease (PLP) domains of coronaviruses (CoV

204 In this study, we focus on the SARS-CoV papain-like protease (PLP), which engages and antagonize

205 ch multifunctional domain is the coronavirus papain-like protease (PLP), which processes the viral re

206 s that are processed by two viral proteases, papain-like protease (PLpro) and 3C-like protease (3CLpr

207 ins (nsps 1 to 16) by two viral proteases, a papain-like protease (PLpro) and a 3C-like protease (3CL

208 rs of MERS-CoV replication, we expressed the papain-like protease (PLpro) and the 3-chymotrypsin-like

209 teracting innate immunity, we identified the papain-like protease (PLpro) domain as a potent IFN anta

210 The papain-like protease (PLpro) domain from the deadly Midd

211 mmediately adjacent to the N-terminus of the papain-like protease (PLpro) domain in coronavirus polyp

212 timization of a potent inhibitor against the papain-like protease (PLpro) from the coronavirus that c

213 nhibitors with nanomolar potency against the papain-like protease (PLpro) from the SARS coronavirus (

214 cute respiratory syndrome (SARS) coronavirus papain-like protease (PLpro) is a DUB that cleaves ISG15

215 efficacy of inhibitors directed against the papain-like protease (PLpro) of severe acute respiratory

216 part of its viral genome, MERS-CoV encodes a papain-like protease (PLpro) that has been observed to a

217 ry syndrome coronavirus (MERS-CoV), encode a papain-like protease (PLpro) that possesses the ability

218 dulators encoded by the SARS-CoV genome: the papain-like protease (PLPro), nonstructural protein 1 (n

219 a chymotrypsin-like protease (3CLpro) and a papain-like protease (PLpro).

220 ong arteriviruses in having three N-terminal papain-like protease 1 (PLP1) domains.

221 ly linked domains of MHV nsp3, including the papain-like protease 2 (PLP2) catalytic domain, the ubiq

222 e an ovarian tumor (OTU) domain DUB known as papain-like protease 2 (PLP2).

223 native processing independent of the encoded papain-like protease activities.

224 rocessing pathway independent of the encoded papain-like protease activities.

225 f ORF3 interactions with the viral helicase, papain-like protease and methylase, which suggest a regu

226 ike protease, and ORF3 interactions with the papain-like protease and putative replicase components:

227 The protein contains a papain-like protease domain (PLP2) that plays a crucial

228 Interestingly, a conserved papain-like protease domain similar to a multifunctional

229 More interestingly, we detected a conserved papain-like protease domain that commonly exists in ssRN

230 We performed bioinformatics analysis on 16 papain-like protease domains from nine different coronav

231 The SARS-CoV papain-like protease is encoded next to SUD within nonst

232 the in vivo efficacy of an inhibitor of the papain-like protease of severe acute respiratory syndrom

233 The papain-like protease p29, derived from the N-terminal po

234 The combined results suggest that papain-like protease p48 plays an essential role in the

235 conserved domain adjacent to the coronavirus papain-like protease, altered the viral protease activit

236 the chimeric-virus platform to evaluate the papain-like protease/deISGylating activity of Middle Eas

237 proteins 1 to 3 are processed by one or two papain-like proteases (PLP1 and PLP2) at specific cleava

238 polyprotein 1a is predicted to encode three papain-like proteases (PLP1alpha, PLP1beta, and PLP1gamm

239 locking the secrets of how coronavirus (CoV) papain-like proteases (PLpros) perform their multifuncti

240 s multiple structural domains, including two papain-like proteases (PLPs) and a highly conserved ADP-

241 oronavirus (MERS-CoV) encode multifunctional papain-like proteases (PLPs) that have the ability to pr

242 ase gene products and characterize two viral papain-like proteases (PLPs), PLP1 and PLP2, which proce

243 roteases via its carboxy-extended domain and papain-like proteases by its amino-terminal domain.

244 scribe a novel tool for studying the role of papain-like proteases in diverse biologic phenomena and

245 Rcr3 and Pip1 are paralogous secreted papain-like proteases of tomato.

246 e position of the canonical catalytic Cys of papain-like proteases, and the function of SERA5 or whet

247 fungus Cryphonectria parasitica, encodes two papain-like proteases, p29 and p48.

248 d on analogy with inhibitor complexes of the papain-like proteases, we propose a model for the substr

249 (MHV), nsps 1, 2, and 3 are processed by two papain-like proteinase activities within nsp3 (PLP1 and

250 domain located immediately downstream of the papain-like proteinase domain.

251 ensively processed by three proteinases, two papain-like proteinases (PLPs), termed PLP1 and PLP2, an

252 to proteolytically modify the SERA family of papain-like proteins.

253 ole OcXII gene presented higher legumain and papain-like proteolytic activities, resulting in a faste

254 in Z, which are both cysteine proteases of a papain-like structure.

255 s from other sources have the hallmarks of a papain-like, Clan CA Cys protease.

256 After exposure to the natural allergen papain, mice selectively lacking the miR-17 approximatel

257 immunization with ovalbumin (OVA) along with papain or alum.

258 EKTI did not inhibit the cysteine proteinase papain or cathepsin K, L, or S.

259 ective inhibition of cathepsin L compared to papain or elastase.

260 ce interleukin 13 (IL-13) when stimulated by papain or house dust mite extract (HDM) and induce eosin

261 eras were treated with the protease allergen papain or the cytokines IL-25 and IL-33 or infected with

262 rface of the support then being treated with papain (or a related agent) to release and remove their

263 n with other proteases such as chymotrypsin, papain, or cathepsin B.

264 sted with proteases such as trypsin, pepsin, papain, or endopeptidase Gly-C.

265 Sensitization to protease allergens, such as papain, or helminth infection is associated with basophi

266 eg cells, thereby suppressing development of papain- or IL-33-induced airway eosinophilia.

267 Sodium caseinate (NaCas) was hydrolyzed by papain, pancreatin and trypsin from 10 min to 24h, and t

268 Subcutaneous immunization with papain plus antigen induced reactive oxygen species (ROS

269 ase (CpL-PME; EC 3.1.1.11) from a commercial papain preparation.

270 ubiquitin recognition and a variation on the papain protease catalytic site configuration that appear

271 Although a member of the papain protease superfamily, Gly m Bd 30 K has a glycine

272 ven within these families of proteins (e.g., papain-related Cys-dependent hydrolases and rhodanese/Cd

273 ubunit with some of the BK channels and that papain removes inactivation by cleaving extracellular si

274 -Lys-Thr-Phe-Cys]-OH (11), starting with the papain-resolved Fmoc-DAgl(Boc).

275 We test papain's HLA class I removing activity under recognized

276 The mechanism of papain's immunogenic activity remains unknown.

277 The activity of papain's substrate selectivity was tested using both a t

278 These findings suggest that papain's targeted enzymatic cleavage of donor HLA class

279 The hH1 region(s) responsible for this papain sensitivity was localised by testing a series of

280 Experiments performed in the absence of papain showed that the activation voltages of the double

281 Intranasal administration of papain stimulated ILC2s and Th2 cells, causing allergic

282 btilisin subfamilies of serine proteases and papain subfamily of cysteine proteases.

283 Finally, studies with the cysteine protease, papain, suggest that the reduction of sulfinamide to the

284 Cysteine proteases of the papain superfamily are implicated in a number of cellula

285 psin S, a lysosomal cysteine protease of the papain superfamily, has been implicated in the preparati

286 psin K, a lysosomal cysteine protease of the papain superfamily, is abundantly and selectively expres

287 t induce T helper type 1 (Th1) responses, or papain that induces T helper type 2 (Th2) responses.

288 d for cathepsin K, while for cathepsin B and papain, the values were 2-4 orders of magnitude lower.

289 xpanded in response to the protease allergen papain, they produced ILC3 but not ILC2 cytokines and ca

290 , and the captured material was treated with papain to generate Fab and Fc for LC/MS analysis.

291 The potential for XCP1 and papain to perform common functions as catalysts of autol

292 Papain-triggered innate immune responses were dependent

293 lter cell surface charge, including trypsin, papain, tunicamycin, neuraminidase, and polybrene, allow

294 The activity of papain was also tested at 4 degrees C, the temperature o

295 ctivated receptor (PAR)-2; TSLP induction by papain was partially dependent on PAR-2.

296 Papain was the enzyme of choice, based on in silico anal

297 water fish (Cirrhinus mrigala) muscle, using papain, were investigated.

298 f IdeS are even more potent as inhibitors of papain, whereas smaller analogues that are active inhibi

299 of dionain-1 was largely similar to that of papain with a preference for hydrophobic and aliphatic r

300 erlase (WPH-Ever; zeta-potential, -39mV) and papain (WPH-Pap; zeta-potential, -7mV), during simulated