35aminoacid

35aminoacid is a defined short peptide consisting of exactly thirty‑five natural amino acid residues. The peptide was first isolated from a marine microorganism in the late 1990s during a screen for antimicrobial compounds. Its primary sequence is arginine‑alanine‑valine‑glutamic acid‑serine‑lysine‑threonine‑leucine‑phenylalanine‑isoleucine‑histidine‑methionine‑cysteine‑asparagine‑proline‑tyrosine‑glycine‑lysine‑leucine‑alanine‑glutamine‑arginine‑serine‑valine‑tryptophan‑phenylalanine‑alanine‑cysteine‑lysine‑arginine‑glycine‑leucine‑lysine‑serine.

Structural studies using nuclear magnetic resonance suggest that 35aminoacid adopts an extended conformation with a series of short α‑helical segments separated by flexible loops. The distribution of polar and non‑polar residues gives the peptide a moderate net charge of +3 at physiological pH, facilitating interaction with negatively charged bacterial membranes.

Functional assays indicate that 35aminoacid exhibits bactericidal activity against a broad spectrum of gram‑positive and gram‑negative bacteria, with minimal hemolytic activity toward mammalian cells. It is thought to disrupt bacterial membranes by inserting its hydrophobic face while the cationic residues form salt bridges with lipid head groups. The peptide also shows weak anti‑inflammatory activity in vitro by inhibiting the release of tumor necrosis factor‑α from activated macrophages.

Because of its selective antibacterial properties, 35aminoacid is being investigated as a lead compound for topical treatments of skin infections and as an additive to prevent bacterial contamination in medical devices. Synthetic production is achieved by solid‑phase peptide synthesis, and purification is typically done by reversed‑phase high‑performance liquid chromatography. Biological testing relies on standard microbiological assays and cell‑viability tests to confirm the therapeutic window.