NDLI: Effects of pH on the adsorption of the viral matrix protein M1

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Biochemistry (Moscow) Supplement Series A: Membrane and Cell Biology : Volume 9, Issue 1, January 2015

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Effects of pH on the adsorption of the viral matrix protein M1

Content Provider	Springer Nature Link
Author	Brevv, V. V. Fedorova, N. V. Indenbom, A. V.
Copyright Year	2015
Abstract	Adsorption of the viral matrix protein M1 on a substrate simulating the lipid membrane surface of the influenza virus was studied by surface plasmon resonance (SPR). It was found that a decrease of pH leads to an increase of the time to reach the saturated level of adsorption, despite the growth of its initial rate. Adsorption of M1 is irreversible in acidic and neutral media, but in the first case the saturated level of adsorption depends on the protein concentration. It was observed that despite the adsorption irreversibility, acidification of the solution down to pH 4 leads to a partial protein desorption from the adsorbed layer that was formed at pH 7. The findings suggest pH-induced changes in shape of the adsorbed M1 molecules. In an acidic medium, elongated protein molecules adsorb mostly laterally in dilute solutions and more orthogonally in concentrated ones. In a neutral medium, protein molecules take on a compact conformation in the adsorption layer, and its thickness does not depend on the concentration. Apparently, flexible C-terminal domain of the adsorbed protein plays a major role in the pH-induced conformational change.
Starting Page	84
Ending Page	91
Page Count	8
File Format	PDF
ISSN	19907478
Journal	Biochemistry (Moscow) Supplement Series A: Membrane and Cell Biology
Volume Number	9
Issue Number	2
e-ISSN	19907494
Language	English
Publisher	Pleiades Publishing
Publisher Date	2015-06-17
Publisher Place	Moscow
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	influenza A virus viral matrix protein M1 surface plasmon resonance Cell Biology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Biophysics

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