دورية أكاديمية

Defining the familial fold of the vicilin-buried peptide family

التفاصيل البيبلوغرافية
العنوان: Defining the familial fold of the vicilin-buried peptide family
المؤلفون: Payne, Colton D., Vadlamani, Grishma, Fisher, Mark F., Zhang, Jingjing, Clark, Richard J., Mylne, Joshua S., Rosengren, K. Johan
بيانات النشر: American Chemical Society
سنة النشر: 2020
المجموعة: The University of Queensland: UQ eSpace
مصطلحات موضوعية: Organic Chemistry, Complementary and alternative medicine, Analytical Chemistry, Molecular Medicine, Pharmacology, Drug Discovery, Pharmaceutical Science, 1313 Molecular Medicine, 1602 Analytical Chemistry, 1605 Organic Chemistry, 2707 Complementary and alternative medicine, 3002 Drug Discovery, 3003 Pharmaceutical Science, 3004 Pharmacology
الوصف: Plants and their seeds have been shown to be a rich source of cystine-stabilized peptides. Recently a new family of plant seed peptides whose sequences are buried within precursors for seed storage vicilins was identified. Members of this Vicilin-Buried Peptide (VBP) family are found in distantly related plant species including the monocot date palm, as well as dicotyledonous species like pumpkin and sesame. Genetic evidence for their widespread occurrence indicates that they are of ancient origin. Limited structural studies have been conducted on VBP family members, but two members have been shown to adopt a helical hairpin fold. We present an extensive characterization of VBPs using solution NMR spectroscopy, to better understand their structural features. Four peptides were produced by solid phase peptide synthesis and shown to favor a helix-loop-helix hairpin fold, as a result of the I-IV/II-III ladderlike connectivity of their disulfide bonds. Interhelical interactions, including hydrophobic contacts and salt bridges, are critical for the fold stability and control the angle at which the antiparallel α-helices interface. Activities reported for VBPs include trypsin inhibitory activity and inhibition of ribosomal function; however, their diverse structural features despite a common fold suggest that additional bioactivities yet to be revealed are likely.
نوع الوثيقة: article in journal/newspaper
اللغة: English
تدمد: 0163-3864
1520-6025
العلاقة: orcid:0000-0002-9316-1465; orcid:0000-0002-6807-5426; orcid:0000-0003-4957-6388; orcid:0000-0002-5007-8434; DP190102058; Not set
الإتاحة: https://doi.org/10.1021/acs.jnatprod.0c00594Test
https://espace.library.uq.edu.au/view/UQ:a847bd2Test
رقم الانضمام: edsbas.AAD3C1BB
قاعدة البيانات: BASE