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LL-37

Cathelicidin, hCAP-18, FALL-39, CAP-18

Quick Stats
Studies 2230
Trials 95
Score 3
2017 pubmed 13 citations

Identification and characterization of multifunctional cationic and amphipathic peptides from soybean proteins.

Taniguchi. Masayuki M; Saito. Kengo K; Nomoto. Takafumi T; Namae. Toshiki T; Ochiai. Akihito A; Saitoh. Eiichi E; Tanaka. Takaaki T

Key Findings

  • Glycinin-17, BCAS-16, and BCBS-11 kill Porphyromonas gingivalis and Candida albicans; Glycinin-17 does not affect Propionibacterium acnes or Streptococcus mutans.
  • All three peptides neutralize lipopolysaccharide (LPS) at low micromolar concentrations, comparable to the antibiotic polymyxin B.
  • The peptides stimulate angiogenesis in human endothelial cells at levels similar to the human peptide LL‑37.
  • Glycinin-17 and BCBS-11 cause less than 2% red‑blood‑cell hemolysis even at 500 µM, indicating low toxicity.

Practical Outcomes

  • These soybean‑derived peptides could become natural antimicrobial or anti‑inflammatory ingredients, especially for oral or skin applications, but they are still at the test‑tube stage. Biohackers should wait for safety and dosing studies before trying them as supplements, though the low hemolysis suggests a favorable safety profile for future development.

Summary

Researchers made three positively‑charged, water‑loving peptides from soybean proteins and showed they can kill some bacteria and yeast, neutralize bacterial toxins, and promote blood‑vessel growth, all while causing very little damage to red blood cells.

Abstract

In this study, we identified and chemically synthesized three cationic and amphipathic peptides (Glycinin-17, BCAS-16, and BCBS-11) from soybean proteins. These peptides had high isoelectric points, high positive net charges, and included multiple hydrophobic amino acids. Subsequently, we identified multiple functions of these peptides, including antimicrobial, lipopolysaccharide-neutralizing, and angiogenic activities, and examined their cytotoxic activities against mammalian red blood cells. Glycinin-17, BCAS-16, and BCBS-11 exhibited antimicrobial activity against Porphyromonas gingivalis and Candida albicans whereas Glycinin-17 did not possess antimicrobial effects on Propionibacterium acnes and Streptococcus mutans. Membrane-depolarization assays and flow cytometric analyses showed that the antimicrobial properties of Glycinin-17, BCAS-16, and BCBS-11 against P. gingivalis, P. acnes, and S. mutans were dependent on membrane-disrupting potential. In contrast, major antimicrobial activities of these peptides against C. albicans were dependent on interactions with targets other than cell membranes. Furthermore, chromogenic Limulus amebocyte lysate assays showed that 50% effective concentrations (EC<sub>50</sub> , 0.12-0.31 &#x3bc;M) of these three peptides neutralize LPS with similar potency (EC<sub>50</sub> : 0.11 &#x3bc;M) to that of polymyxin B. Moreover, tube-formation assays in human umbilical vein endothelial cells showed similar angiogenic activities of the three peptides as that following treatment with LL-37. Although BCAS-16 exhibited hemolytic activity, the rate of hemolysis for Glycinin-17 and BCBS-11 in the presence of 500-&#x3bc;M Glycinin-17 and BCBS-11 was less than 2%. These results demonstrate that cationic and amphipathic peptides from soybean proteins, particularly Glycinin-17 and BCBS-11, have potential as multifunctional ingredients for healthcare applications.

Study Information

Provider

pubmed

Year

2017

Date

2017-07-01T00:00:00.000Z

DOI

10.1002/bip.23023

Citations

13

References

54