A novel synthetic peptide analog enhanced antibacterial activity of the frog-derived skin peptide wuchuanin-A1

Abstract

In recent years, there has been a growing focus on the development of novel antibacterial compounds for clinical applications, such as antimicrobial peptide (AMP). Among the developed AMP, wuchuanin-A1, a coil-shaped bioactive peptide derived from Odorrana wuchuanensis frog skin, has been reported to exhibit antibacterial, antifungal, and antioxidant activity, but there are limited studies on its potential as an antibacterial agent. Therefore, this study aims to molecularly modify the sequence of wuchuanin-A1 to enhance its antibacterial properties. The interaction of both the native and analog peptide with bacterial inner membranes was initially assessed using computational methods. Specific amino acid substitutions were then used to enhance the modified peptide’s antibacterial efficacy, followed by several preliminary tests to evaluate its activity. This study bridges the gap in exploring the potential of wuchuanin-A1 for antibacterial purposes, providing insights into the design of effective antimicrobial agents.

Communicated by Ramaswamy H. Sarma

Keywords:

• AMP
• wuchuanin-A1
• peptide analog

Acknowledgments

We would also like to express our gratitude to Universitas Gadjah Mada for providing us with licenses for Wolfram Mathematica 13.3.

Disclosure statement

No potential conflict of interest was reported by the author(s).

Authors’ contributions

RAP carried out the experiments, analyzed the results, and drafted the manuscript. RTS, MSR, and TJR conceived the study and actively contributed to its coordination. All of the authors have thoroughly reviewed and approved the final manuscript.

Additional information

Funding

The authors are grateful for the funding support from the Ministry of Education, Culture, Research, and Technology for funding this study through the Master’s Education Scholarship Program towards the Doctorate for Excellent Undergraduates (PMDSU) program with contract [number 089/E5/PG.02.00.PT/2022; 1999/UN1/DITLIT/Dit-Lit/PT.01.03/2022].