PT  - JOURNAL ARTICLE
AU  - Sikdar, Samapan
AU  - Banerjee, Manidipa
AU  - Vemparala, Satyavani
TI  - Role of Disulfide Bonds in Membrane Partitioning of a Viral Peptide
AID  - 10.1101/2021.09.21.461184
DP  - 2021 Jan 01
TA  - bioRxiv
PG  - 2021.09.21.461184
4099  - http://biorxiv.org/content/early/2021/09/21/2021.09.21.461184.short
4100  - http://biorxiv.org/content/early/2021/09/21/2021.09.21.461184.full
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.