Lipid Transfer Proteins (LTPs) Partially Purified from Capsicum chinense Jacq. Seeds: Antifungal Properties and α-amylase Inhibitory Activity

被引：0

作者：

Oliveira, Arielle Pinheiro Bessiatti Fava ^{[1
]}

Resende, Larissa Maximiano ^{[1
]}

da Silva, Marciele Souza ^{[1
]}

dos Santos, Layrana de Azevedo ^{[1
]}

Carvalho, Andre Oliveira ^{[1
]}

Chaves, Renata Pinheiro ^{[2
]}

Nagano, Celso Shiniti ^{[2
]}

Moreira, Felipe Figueiroa ^{[3
]}

Seabra, Sergio Henrique ^{[3
]}

Da Cunha, Maura ^{[3
]}

Mello, Erica de Oliveira ^{[1
]}

Taveira, Gabriel Bonan ^{[1
]}

Rodrigues, Rosana ^{[4
]}

Gomes, Valdirene Moreira ^{[1
,5
]}

机构：

[1] Univ Estadual Norte Fluminense, Ctr Biociencias & Biotecnol, Lab Fisiol & Bioquim Microrganismos, Campos Dos Goytacazes, RJ, Brazil

[2] Univ Fed Ceara, Dept Engn Pesca, Lab Bioquim Marinha, Fortaleza, CE, Brazil

[3] Univ Estadual Norte Fluminense Darcy Ribeiro UENF, Ctr Biociencias & Biotecnol, Lab Biol Celular & Tecidual, Campos Dos Goytacazes, RJ, Brazil

[4] Univ Estadual Norte Fluminense, Ctr Ciencias & Tecnol Agr, Lab Melhoramento & Genet Vegetal, Campos Dos Goytacazes, RJ, Brazil

[5] Univ Estadual Norte Fluminense, Ctr Biociencias & Biotecnol, BR-28015602 Campos Dos Goytacazes, RJ, Brazil

来源：

PROTEIN JOURNAL | 2025年 / 44卷 / 02期

关键词：

Antimicrobial peptide; Capsicum; Candida; LTP; -alpha-amylase; PEPTIDES; PEPPER;

D O I：

10.1007/s10930-025-10256-x

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

In this study, we identified and partially purified antimicrobial peptides belonging to the family of lipid transfer proteins (LTPs) from Capsicum chinense seeds (UENF 1751 accession). Fractions rich in LTPs were obtained via ion exchange chromatography and subsequently purified via reverse-phase chromatography in an HPLC system. Therefore, two fractions were revealed: C1 (the nonretained fraction) and C2 (the retained fraction in ion-exchange chromatography). Fraction C1 was subjected to reverse-phase chromatography via a C18 column on an HPLC system, and ten fractions were obtained (P1-P10), all of which significantly inhibited the growth of Candida albicans, except for P4 and P9. The viability analysis of the active fractions at a concentration of 100 mu g.mL-1 against C. albicans revealed that they did not exhibit fungicidal activity but rather exhibited fungistatic activity. The peptide is considered fungicidal when it results in the total loss of viable yeast cells, that is, when it causes the complete death of the fungi. When the substance only inhibits cell growth, but does not eliminate them completely, the effect is classified as fungistatic. Fractions P3, P4, P7, and P10 inhibited Tenebrio molitor larvae alpha-amylase. The P10 fraction presented protein bands in its electrophoretic profile with a molecular mass between 6.5 kDa and 14.2 kDa and reacted positively to an antibody produced against a protein from the LTP family bywestern blotting. The results of the analysis of amino acid residues from the P10 fraction revealed similarity between type I LTPs and type II LTPs. The ultrastructural aspects of C. albicans cells exposed to the P10 fraction were evaluated via transmission electron microscopy (TEM), with significant differences in their morphology being evident compared with those of the control. In summary, our results demonstrated the presence of LTPs in C. chinense seeds with inhibitory effects on the growth of yeasts of the genus Candida, which exhibited fungistatic effects and structural changes in C. albicans cells, in addition to exhibiting inhibitory effects on the larval insect T. molitor alpha-amylase.

引用

页码：201 / 212

页数：12

共 38 条

[1] Potent Anti-Candida Fraction Isolated from Capsicum chinense Fruits Contains an Antimicrobial Peptide That is Similar to Plant Defensin and is Able to Inhibit the Activity of Different α-Amylase Enzymes [J].