Membrane-Bound Conformations of Antimicrobial Agents and Their Modes of Action

Baul, Upayan; Vemparala, Satyavani

doi:10.1016/bs.adplan.2015.06.006

Cited by 5 publications

(7 citation statements)

References 143 publications

(231 reference statements)

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“…A majority of existing simulation studies on viroporins are related to membrane embedded states focusing on their preferred oligomeric arrangements [6,[18][19][20][21], channel/pore activity [22][23][24][25] and drug binding [26][27][28], to name a few. On other hand, atomistic and coarsegrained MD simulations of antimicrobial peptides [29][30][31][32][33][34][35][36] and fusion peptides [37][38][39][40][41][42][43] of enveloped-virus origin have explored peptide entry through partitioning and insertion into membranes. These studies provide detailed insight into effect of lipid type and composition on peptide-membrane modes of interaction and subsequent membrane reorganization by these membrane active peptides.…”

Section: Introductionmentioning

confidence: 99%

Effect of cholesterol on the membrane partitioning dynamics of hepatitis A virus-2B peptide

2021

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Section: Introductionmentioning

confidence: 99%

Effect of cholesterol on the membrane partitioning dynamics of hepatitis A virus-2B peptide

2021

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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

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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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Membrane-Bound Conformations of Antimicrobial Agents and Their Modes of Action

Cited by 5 publications

References 143 publications

Effect of cholesterol on the membrane partitioning dynamics of hepatitis A virus-2B peptide

Effect of cholesterol on the 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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