Influence of microenvironment and liposomal formulation on secondary structure and bilayer interaction of lysozyme

Witoonsaridsilp, Wasu; Panyarachun, Busaba; Sarisuta, Narong; Müller‐Goymann, Christel C.

doi:10.1016/j.colsurfb.2009.09.027

Cited by 17 publications

(8 citation statements)

References 44 publications

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“…4a) showed that the secondary structure of LYS in solution was the same at pH 2.0 and 7.0 and that it was not altered in the presence of PC. These results agree with Witoonsaridsilp, Panyarachun, Sarisuta, and Müller-Goymann (2010), who reported that the secondary structure of LYS entrapped in non-charged and negatively-charged liposomes, with various lipid compositions, does not significantly differ from that in buffer solutions at different pH values. The near-UV CD spectrum of LYS at pH 2.0 was typical of this protein, which does not change with respect to the neutral pH condition (Fig.…”

Section: Effect Of the Presence Of Pc On The Gastric Digestion Of Lyssupporting

confidence: 95%

“…On the other hand, LYS, with an isoelectric point near 11, is a highly electropositive protein, that can easily penetrate anionic phospholipid vesicles, such as those formed by phosphatidylserine or phosphatidylglycerol. In this case, LYS binding to anionic vesicles is governed by electrostatic effects that lead to LYS penetration into the lipid phase (Mudgil et al, 2006;Witoonsaridsilp et al, 2010).…”

Section: Effect Of the Presence Of Pc On The Gastric Digestion Of Lysmentioning

confidence: 98%

“…Nevertheless, LYS could still interact with zwitterionic phospholipids, such as PC, through hydrophobic and polar interactions that could lead to LYS association to PC films. In fact, it has been reported that LYS could be entrapped in non-charged PC liposomes (Witoonsaridsilp et al, 2010). However, penetration is difficult once adsorption has occurred, because LYS is excluded from interacting with the hydrophobic portion of the lipid below the chain transition temperature of PC, which is approximately 41°C (Mudgil, Torres, & Millar, 2006).…”

Section: Effect Of the Presence Of Pc On The Gastric Digestion Of Lysmentioning

confidence: 99%

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Susceptibility of lysozyme to in-vitro digestion and immunoreactivity of its digests

et al. 2011

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a-LactalbuminIn-vitro gastric digestion In-vitro duodenal digestion IgE-binding a b s t r a c t This paper examines lysozyme (LYS) behaviour upon in-vitro digestion, mimicking different conditions in the stomach and intestine, and assessing the effect of natural surfactants, such as phosphatidylcholine (PC) or bile salts (BS), on hydrolysis and residual immunogenicity of the digests. The hydrolysis pattern of LYS was compared to that of a-lactalbumin (LA). Hydrolysis of LYS only occurred at low pH. PC slightly increased its resistance to pepsinolysis. A similar behaviour was found for LA. Circular dichroism revealed that the more rigid structure of LYS, as compared with that of LA, could protect it from proteolysis at acidic pH and fluorescence spectra suggested that, at acidic pH, both proteins associated to PC films. The gastric digests of LYS showed high IgE-binding capacity using sera from egg-allergic patients. On the other hand, it was found that LYS precipitated under conditions that simulated a duodenal environment, mainly due to the presence of BS.Published by Elsevier Ltd.

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Section: Effect Of the Presence Of Pc On The Gastric Digestion Of Lyssupporting

confidence: 95%

Section: Effect Of the Presence Of Pc On The Gastric Digestion Of Lysmentioning

confidence: 98%

Section: Effect Of the Presence Of Pc On The Gastric Digestion Of Lysmentioning

confidence: 99%

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Susceptibility of lysozyme to in-vitro digestion and immunoreactivity of its digests

et al. 2011

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“…17 Immediately after its interaction within the lipid bilayer, lysozyme undergoes conformational changes with subsequent reorganization (oligomerization) that leads to vesicle clustering and amyloid fibril formation. [42][43][44][45] The concomitant presence of these effects contributes to a decrement of the lipid membrane fluidity (1/P).…”

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confidence: 99%

Lysozyme interaction with negatively charged lipid bilayers: protein aggregation and membrane fusion

et al. 2012

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We report on the interaction of hen egg-white lysozyme (HEWL) with lipid vesicles in terms of surfaceinduced protein conformational variation and subsequent aggregation. In particular, we investigated the variations of the secondary structure of native lysozyme in the presence of liposomes with different surface charge density, resulting from different molar ratios of the zwitterionic POPC (1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine) and the negatively charged POPG (1-palmitoyl-2-oleoyl-snglycero-3-phospho-(1 0 -rac-glycerol)). It is well known that the main driving force involved in the interaction between globally anionic liposomes and lysozyme is electrostatic compensation, which, in some cases, produces extended aggregation. Moreover the presence of membranes can induce unfolding in the protein. In order to understand the main determinants of such phenomena, we probed simultaneously lysozyme-induced vesicle fusion events, variations in the secondary structure of the protein and its effect on liposomal membrane fluidity. We found that above a charge-density threshold, the association with vesicles results in modifications of the native structure associated with a decrease of liposomal membrane fluidity. Electron microscopy images revealed that the above described interactions result in mesoscopic structural changes, i.e. liposome clustering and fusion, together with the appearance of elongated structures, reminiscent of fibrillar aggregates. Additionally, a confocal microscopy analysis revealed that upon interaction with giant unilamellar vesicles (GUVs) of the same lipid composition where the above interactions were observed, a prompt insertion of lysozyme in the membrane occurs, leading to vesicle clustering, with the appearance of elongated structures where both the lipid and the protein are present.

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“…Moreover, the sizes of the MANS-BA liposomes with CHOL were significantly larger than those without CHOL (p50.05, independent sample t-test). These results might be due to the fact that CHOL could alter the fluidity of liposomal membrane by rigidity enhancement (Witoonsaridsilp et al, 2010). The quantity of MAN incorporated in MANS-BA proliposome powders did not directly affect the size of liposomes.…”

Section: Particle Sizementioning

confidence: 95%

Enhanced permeability across Caco-2 cell monolayers by specific mannosylating ligand of buserelin acetate proliposomes

Yingsukwattana¹,

Puttipipatkhachorn²,

Ruktanonchai³

et al. 2015

Journal of Liposome Research

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Influence of microenvironment and liposomal formulation on secondary structure and bilayer interaction of lysozyme

Cited by 17 publications

References 44 publications

Susceptibility of lysozyme to in-vitro digestion and immunoreactivity of its digests

Susceptibility of lysozyme to in-vitro digestion and immunoreactivity of its digests

Lysozyme interaction with negatively charged lipid bilayers: protein aggregation and membrane fusion

Enhanced permeability across Caco-2 cell monolayers by specific mannosylating ligand of buserelin acetate proliposomes

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