Structural, optical, and biological properties of L-alanine single crystal by slow evaporation method

Jini, D.; Aravind, M.; Nirmal, L. Jothi; Ajitha, S.

doi:10.1016/j.matpr.2020.11.736

Cited by 2 publications

(2 citation statements)

References 17 publications

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“…Agerberth et al successfully characterized a 39-residue antibacterial peptide exceptionally rich in proline and arginine . The positive ions produced by l -alanine interact with the negative bacterial wall of Gram-negative bacteria resulting in damage to the respiratory system of bacteria and resistance of their growth .…”

Section: Resultsmentioning

confidence: 99%

“…37 The positive ions produced by L-alanine interact with the negative bacterial wall of Gram-negative bacteria resulting in damage to the respiratory system of bacteria and resistance of their growth. 38 L-Methionine (MET) improves the durability of antibacterial cotton fabrics. 39 The main reason for the antibacterial effect of hydrophobic amino acids is probably the specific structure of the amino acids.…”

Section: Resultsmentioning

confidence: 99%

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Harsh Sensitivity and Mechanism Exploration of an Antibacterial Peptide Extracted from Walnut Oil Residue Derived from Agro-Industrial Waste

Liu

Meng

et al. 2022

J. Agric. Food Chem.

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Walnut (Juglans regia L.) cake meal constitutes a significant amount of solid byproduct from the production of walnut oil, comprising more than 40% protein. However, it is usually not well utilized. Therefore, an antibacterial peptide was obtained by hydrolyzing walnut oil residue protein with pepsin based on the diameter parameters of the antibacterial zone in this research. The purified antibacterial peptide WRPH-II-6 was obtained by two-part purification (ultrafiltration and reversed-phase liquid chromatography) and possessed higher antibacterial activity against Escherichia coli (MIC = 1.33 mg/mL), Staphylococcus aureus (MIC = 0.33 mg/mL), and Bacillus subtilis (MIC = 0.66 mg/mL). The amino acid sequence of WRPH-II-6 was identified as TGSAVPSPRASATATMEMAAAMGLMPGSPSSVSAVMSPF, where the presence of a large proportion of hydrophobic amino acid residues, such as alanine, proline, and methionine, explained the marked antibacterial activity of WRPH-II-6. The harsh sensitivity experiment demonstrated that WRPH-II-6 retains the stability of antibacterial activity when exposed to broad-spectrum pH values, variable temperatures, and long-lasting UV irradiation. The antibacterial mechanism of the WRPH-II-6 peptide against S. aureus and B. subtilis involves nonmembrane disruption: the contact of anions and cations causes the folding and collapse of the bacterial cell membrane to achieve the inhibitory effect. The antibacterial mechanism against E. coli is membrane disruption, which markedly disrupts the bacterial cell membrane to achieve the bactericidal effect. Significantly, the walnut residual protein hydrolysate is a potent preservative and antibacterial agent.

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Section: Resultsmentioning

confidence: 99%