海洋巨藻crisdrus蛋白水解物活性肽对金黄色葡萄球菌的抑菌活性

IF 1.1 Q4 PHARMACOLOGY & PHARMACY Pharmacia Pub Date : 2023-10-05 DOI:10.3897/pharmacia.70.e112215
Ahmad Habibie, Tri Joko Raharjo, Respati Dwi Swasono, Endah Retnaningrum
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引用次数: 0

摘要

巨藻是一种具有生产抗菌肽(AMPs)潜力的蛋白质来源,具有广泛的生物活性。本研究旨在从海洋巨藻crispus蛋白水解物中寻找具有生物活性的肽类抗菌化合物。用强阳离子交换剂固相萃取法从胰蛋白酶和α -糜蛋白酶水解产物中分离出肽。水解蛋白的某些部分表现出良好的抑制区,在pH 9下洗脱的α-胰凝乳酶消化部分对革兰氏阴性菌金黄色葡萄球菌的抑制作用最高。部分多肽为阳离子螺旋多肽,疏水性百分比为16.67 ~ 77.78%。经鉴定,潜在抗菌肽P01 KKNVTTLAPLVF为α -螺旋阳离子抗菌肽,肉汁值0.525,结构为两亲性,总电荷为+2。此外,P07 sagsgignosgw和P20 RTASSR肽与金黄色葡萄球菌DNA旋切酶和DHFR受体的相互作用较强,结合能分别为-8.0和-7.3 kcal/mol。
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Antibacterial activity of active peptide from marine macroalgae Chondrus crispus protein hydrolysate against Staphylococcus aureus
Macroalgae is a protein source with the potential to yield antimicrobial peptides (AMPs) that exhibit a wide range of biological activities. This study aimed to find bioactive peptide-based antibacterial compounds from marine macroalgae Chondrus crispus protein hydrolysate. The peptides were isolated by solid phase extraction with a strong cation exchanger from trypsin-digested and α -chymotrypsin-digested hydrolysates. Certain fractions of the hydrolyzed protein displayed a good inhibition zone, with the α-chymotrypsin-digested fraction eluted at pH 9 exhibiting the highest inhibition against Gram-negative bacteria Staphylococcus aureus . Several peptides were characterized as cationic helical peptides with hydrophobicity percentages of 16.67–77.78%. The potential antibacterial peptide P01 KKNVTTLAPLVF was identified as an α -helical cationic antibacterial peptide with 0.525 GRAVY value, amphipathic structure, and +2 total charge. Moreover, strong interaction was observed between P07 SAGSGNEGLSGW and P20 RTASSR peptide with DNA gyrase and DHFR receptors from S. aureus with binding energy -8.0 and -7.3 kcal/mol, respectively.
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来源期刊
Pharmacia
Pharmacia PHARMACOLOGY & PHARMACY-
CiteScore
2.30
自引率
27.30%
发文量
114
审稿时长
12 weeks
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