Influences of disulfide connectivity on structure and antimicrobial activity of tachyplesin I

Shi, Juan; So, Lok Yan; Chen, Fangling; Liang, Jiazhen; Chow, Ho Yin; Wong, Kwok Yin; Wan, Shengbiao; Jiang, Tao; Yu, Rilei

doi:10.1002/psc.3087

Cited by 10 publications

(10 citation statements)

References 32 publications

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“…Evidence of thiol–disulphide redox status-dependent exposure of hydrophobic patches facilitating peptide partitioning is well documented through experimental investigations on different membrane-active agents, like antimicrobial peptides (Schroeder et al 2011 ; Sharma & Nagaraj 2015 ; Shi et al 2018 ; Zhang 2020 ) and viral peptides (Abell & Brown, 1993 ; Binley James et al 2003 ; Gallagher 1996 ; Jain et al 2007 ; Key et al 2015 ; Locker & Griffiths 1999 ; Moyer & Nemerow 2012 ; Wallin et al 2004 ; Zokarkar et al 2012 ). This importance of disulphide bond in mediating viral peptide partitioning and subsequent entry into host cells is currently being explored to design antiviral agents.…”

Section: Discussionmentioning

confidence: 99%

“…Further, molecular dynamics (MD) simulation studies of hBD-3 analogues lacking SS-linkages induce significant disruption of negatively charged lipid bilayers, compared to their native counter-part (Zhang 2020 ). Similarly, the antimicrobial activity of other disulphide-rich peptides has been known to be regulated by presence / absence of SS-bonds (Doherty et al 2006 ; Lipkin & Lazaridis 2015 ; Rodnin et al 2020 ; Shi et al 2018 ).…”

Section: Introductionmentioning

confidence: 99%

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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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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Role of Disulphide Bonds in Membrane Partitioning of a Viral Peptide

2022

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“…Evidence of thiol-disulfide redox status dependent exposure of hydrophobic patches facilitating peptide partitioning is well documented through experimental investigations on different membrane active agents like antimicrobial peptides [10,11,13,17] and viral fusion peptides [21,[23][24][25][26][27][28][29]31]. This importance of disulfide bond in mediating viral peptide partitioning and subsequent entry into host cells is currently being explored to design antiviral agents.…”

Section: Discussionmentioning

confidence: 99%

“…[13] Similarly, the antimicrobial activity of other disulfide rich peptides has been known to be regulated by presence / absence of SS-bonds. [15][16][17][18] Environment dependent thiol-disulfide switching plays important role in mediating virus entry into cells. [9] In this regard, it is required for Human immunodeficiency virus-1 (HIV-1) envelope protein dissociate into two subunits namely, gp120 and gp41, upon interaction with host cell receptors followed by reduction of redox active SS-bonds to allosterically unmask membrane active fusion peptide initiating membrane insertion.…”

Section: Introductionmentioning

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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“…The purified linear peptides 2, 3, and 4 were folded by the two-step oxidative folding strategy. 45,46 Briefly, linear peptide 2 (24 mg, 50 μM) was dissolved in 80 ml of 10% acetonitrile in water (v/v) solution.…”

Section: The Two-step Oxidative Folding Of Peptides 2 3 Andmentioning

confidence: 99%

DIC/Oxyma‐based accelerated synthesis and oxidative folding studies of centipede toxin RhTx

Chen

Wang

et al. 2021

Journal of Peptide Science

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Coupling reagents play crucial roles in the iterative construction of amide bonds for the synthesis of peptides and peptide-based derivatives. The novel DIC/Oxyma condensation system featured with the low risk of explosion displayed remarkable abilities to inhibit racemization, along with efficient coupling efficiency in both manual and automated syntheses. Nevertheless, an ideal reaction molar ratio in DIC/Oxyma condensation system and the moderate reaction temperature by manual synthesis remain to be further investigated. Herein, the synthetic efficiencies of different reaction ratios between DIC and Oxyma under moderate reaction temperature were systematically evaluated. The robustness and efficiency of DIC/Oxyma condensation system are validated by the rapid synthesis of linear centipede toxin RhTx. Different folding strategies were applied for the construction of disulfide bridges in RhTx, which was further confirmed in assays of circular dichroism and patch-clamp electrophysiology evaluation. This work establishes the DIC/Oxyma-based accelerated synthesis of peptides under moderate condensation conditions, which is especially useful for the manual synthesis of peptides. Besides, the strategy presented here provides robust technical supports for the large-scale synthesis and oxidative folding of RhTx.

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Influences of disulfide connectivity on structure and antimicrobial activity of tachyplesin I

Cited by 10 publications

References 32 publications

Role of Disulphide Bonds in Membrane Partitioning of a Viral Peptide

Role of Disulphide Bonds in Membrane Partitioning of a Viral Peptide

Role of Disulfide Bonds in Membrane Partitioning of a Viral Peptide

DIC/Oxyma‐based accelerated synthesis and oxidative folding studies of centipede toxin RhTx

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