Antimicrobial Peptides: Potential Therapeutic Substitute for Antibiotics in Helicobacter pylori Infection

Article information

Korean J Helicobacter Up Gastrointest Res. 2026;26(1):1-2

Publication date (electronic) : 2026 March 5

doi : https://doi.org/10.7704/kjhugr.2026.0005

Seokin Kang

Department of Internal Medicine, Ilsan Paik Hospital, Inje University College of Medicine, Goyang, Korea

Corresponding author Seokin Kang, MD, PhD Department of Internal Medicine, Ilsan Paik Hospital, Inje University College of Medicine, 170 Juhwa-ro, Ilsanseo-gu, Goyang 10380, Korea E-mail: seokinkang@paik.ac.kr

Received 2026 January 16; Revised 2026 January 26; Accepted 2026 January 28.

Antimicrobial peptide (AMP) is a short, amphipathic polypeptide composed of fewer than 50 amino acids and with a molecular weight of less than 10 kDa. These peptides are produced by a wide variety of organisms and play an important role in the innate immune system. They constitute a first-line defense against microbial invasion and exhibit broad-spectrum activity against bacteria, fungi, and viruses and are also effective against multidrug-resistant bacteria [1,2].

With the increasing antibiotic resistance of Helicobacter pylori in recent years, the effectiveness of antibiotic therapy has declined, prompting the search for alternative antimicrobial strategies. In this context, some AMPs—including pexiganan, tilapia piscidins, epinecidin‐1, cathelicidins, defensins, bicarinalin, odorranain‐HP, PGLa‐AM1, and bacteriocins—have been identified and investigated for their anti-H. pylori activity [3]. Advances in computational approaches, such as bioinformatics, molecular docking, and molecular dynamic simulation, have accelerated the drug discovery process.

In this study [4], AMP variants derived from Lactobacillus species were explored using an in-silico approach. From 109 AMPs retrieved from multiple databases, nine (seq28, seq30, seq55, seq78, seq79, seq9v1, seq9v2, seq9v3, and seq9v4) were shortlisted based on anti-cancer and anti-inflammatory peptide predictions, antigenicity analysis, and ADMET properties analysis. Docking analyses were then conducted between the 9 AMPs and 4 target virulence proteins (CagA, BabA, SabA, and VacA), along with their corresponding 14 interacting host proteins implicated in gastric carcinogenesis. Among the shortlisted peptides, four (seq28, seq30, seq55, and seq78) emerged as candidates with potential for targeting H. pylori.

Although the findings are limited to computational predictions and require further in vitro and in vivo validation, this study provides a structured framework for identifying AMP candidates that may serve as alternatives to antibiotics. In the post-antibiotic era, AMPs continue to attract attention as potential therapeutic alternatives [3], and this study offers a useful starting point for future translational research aimed at developing new strategies to manage H. pylori infections.