Interdigitation of Lipids Induced by Membrane–Active Proteins

Devanand, T; Krishnaswamy, S.; Vemparala, Satyavani

doi:10.1007/s00232-019-00072-7

Cited by 13 publications

(9 citation statements)

References 100 publications

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“…Peptide insertion is often driven by membrane induced partitioning, widely reported for antimicrobial peptides [30,34,55], polymers [31-33, 35, 36, 57] and other membrane active molecules [58][59][60]. We confirm this by computing equilibrium density profiles of peptide and membrane components along the bilayer normal (z-axis).…”

Section: Peptide-membrane Mode Of Interactionsupporting

confidence: 68%

Effect of Cholesterol on Membrane Partitioning Dynamics of Hepatitis A Virus-2B peptide

Sikdar

Banerjee

Vemparala

2020

Preprint

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Understanding the viral peptide detection, partitioning and subsequent host membrane composition-based response is required for gaining insights into viral mechanism. Here, we probe the crucial role of presence of membrane lipid packing defects, depending on the membrane composition, in allowing the viral peptide belonging to C-terminal Hepatitis A Virus-2B (HAV-2B) to detect, attach and subsequently partition into the host cell membrane mimics. We conclusively show that the hydrophobic residues in the viral peptide detect the transiently present lipid packing defects, insert themselves into such defects, form anchor points and facilitate the partitioning of the peptide. We also show that the presence of cholesterol significantly alters such lipid packing defects, both in size and in number, thus mitigating the partitioning of the membrane active viral peptide into cholesterol-rich membranes. These results show differential ways in which presence and absence of cholesterol can alter the permeability of the host membranes to the membrane active viral peptide component of HAV-2B virus, via lipid packing defects, and can possibly be a part of general membrane detection mechanism for the viroporin class of viruses.

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Section: Peptide-membrane Mode Of Interactionsupporting

confidence: 68%

Effect of Cholesterol on Membrane Partitioning Dynamics of Hepatitis A Virus-2B peptide

Sikdar

Banerjee

Vemparala

2020

Preprint

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“…The conformation of SS-free HAV-2B peptide is such that it acquires a strong facially amphipihilic character upon segregation of hydrophobic and hydrophilic residues. Different membrane-active agents including antimicrobial peptides (Leontiadou et al 2006 ; Mondal et al 2010 ; Vanni et al 2014 ), polymers (Baul et al 2014 ; Baul & Vemparala, 2015 , 2017 ; Palermo et al 2012 , 2013 ; Rahman et al 2018 ; Rani et al 2021 ) and other membrane-active molecules (Devanand et al 2019 ; Polley & Vemparala, 2013 ; Vemparala et al 2006 ) are known to acquire such amphipihilic conformations upon partitioning into cellular membranes. However, in SS11-47 (Fig.…”

Section: Discussionmentioning

confidence: 99%

Role of Disulphide Bonds in Membrane Partitioning of a Viral Peptide

2022

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The importance of disulphide bond in mediating viral peptide entry into host cells is well known. In the present work, we elucidate the role of disulphide (SS) bond in partitioning mechanism of membrane-active Hepatitis A Virus-2B (HAV-2B) peptide, which harbours three cysteine residues promoting formation of multiple SS-bonded states. The inclusion of SS-bond not only results in a compact conformation but also induces distorted α-helical hairpin geometry in comparison to SS-free state. Owing to these, the hydrophobic residues get buried, restricting the insertion of SS-bonded HAV-2B peptide into lipid packing defects and thus the partitioning of the peptide is completely or partly abolished. In this way, the disulphide bond can potentially regulate the partitioning of HAV-2B peptide such that the membrane remodelling effects of this viral peptide are significantly reduced. The current findings may have potential implications in drug designing, targeting the HAV-2B protein by promoting disulphide bond formation within its membrane-active region. Graphical Abstract Supplementary Information The online version contains supplementary material available at 10.1007/s00232-022-00218-0

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“…The conformation of SS-free HAV-2B peptide is such that it acquires a strong facially amphipihilic character upon segregation of hydrophobic and hydrophilic residues. Different membrane active agents including antimicrobial peptides [55,62,63], polymers [58,[64][65][66][67][68][69] and other membrane active molecules [70][71][72] are known to acquire such amphipihilic conformations upon partitioning into cellular membranes. However, in SS11-47 (Fig 6C ) and SS11-52 (Fig 6D ) states, the hydrophobic accessible surface area is limited resulting in mitigation of peptide partitioning.…”

Section: Discussionmentioning

confidence: 99%

Role of Disulfide Bonds in Membrane Partitioning of a Viral Peptide

Sikdar

Banerjee

Vemparala

2021

Preprint

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The importance of disulfide bond in mediating viral peptide entry into host cells is well known. In the present work, we elucidate the role of disulfide (SS) bond in partitioning mechanism of membrane active Hepatitis A Virus-2B (HAV-2B) peptide, which harbours three cysteine residues promoting formation of multiple SS-bonded states. The inclusion of SS-bond not only results in a compact conformation but also induces distorted α-helical hairpin geometry in comparison to SS-free state, resulting in reduced hydrophobic exposure. Owing to this, the partitioning of HAV-2B peptide is completely or partly abolished. In a way, the disulfide bond regulates the partitioning of HAV-2B peptide, such that the membrane remodelling effects of this viral peptide are significantly reduced. The current findings may have potential implications in drug designing, targeting the HAV-2B protein by promoting disulfide bond formation within its membrane active region.

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Interdigitation of Lipids Induced by Membrane–Active Proteins

Cited by 13 publications

References 100 publications

Effect of Cholesterol on Membrane Partitioning Dynamics of Hepatitis A Virus-2B peptide

Effect of Cholesterol on Membrane Partitioning Dynamics of Hepatitis A Virus-2B peptide

Role of Disulphide Bonds in Membrane Partitioning of a Viral Peptide

Role of Disulfide Bonds in Membrane Partitioning of a Viral Peptide

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