RT Journal Article SR Electronic T1 Role of Disulfide Bonds in Membrane Partitioning of a Viral Peptide JF bioRxiv FD Cold Spring Harbor Laboratory SP 2021.09.21.461184 DO 10.1101/2021.09.21.461184 A1 Sikdar, Samapan A1 Banerjee, Manidipa A1 Vemparala, Satyavani YR 2021 UL http://biorxiv.org/content/early/2021/09/21/2021.09.21.461184.abstract AB 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.Competing Interest StatementThe authors have declared no competing interest.