Next Article in Journal
Anthocyanins from Hibiscus syriacus L. Inhibit Melanogenesis by Activating the ERK Signaling Pathway
Next Article in Special Issue
Unravelling the Skin Secretion Peptides of the Gliding Leaf Frog, Agalychnis spurrelli (Hylidae)
Previous Article in Journal
Pharmacology Study of the Multiple Angiogenesis Inhibitor RC28-E on Anti-Fibrosis in a Chemically Induced Lung Injury Model
Previous Article in Special Issue
Electro-Acupuncture Alleviates Cisplatin-Induced Anorexia in Rats by Modulating Ghrelin and Monoamine Neurotransmitters
Open AccessArticle

Design of N-Terminal Derivatives from a Novel Dermaseptin Exhibiting Broad-Spectrum Antimicrobial Activity against Isolates from Cystic Fibrosis Patients

1
School of Pharmacy, China Medical University, Shenyang 110001, China
2
Natural Drug Discovery Group, School of Pharmacy, Queen’s University Belfast, Belfast BT9 7BL, Northern Ireland, UK
*
Authors to whom correspondence should be addressed.
Biomolecules 2019, 9(11), 646; https://doi.org/10.3390/biom9110646
Received: 8 October 2019 / Revised: 21 October 2019 / Accepted: 23 October 2019 / Published: 24 October 2019
(This article belongs to the Special Issue Peptides: Molecular and Biotechnological Aspects)
Dermaseptins are an antimicrobial peptide family widely identified from the skin secretions of phyllomeudusinae frogs. Here, we identify Dermaseptin-PC (DM-PC), from the skin secretion of Phyllomedusa coelestis, and further investigate the properties of this peptide, and a number of rationally designed truncated derivatives. The truncated 19-mer derived from the N-terminus exhibited similar antimicrobial potency when compared to the parent peptide, but the haemolytic effect of this truncated peptide was significantly decreased. Based on previous studies, the charge and hydrophobicity of truncated derivatives can affect the bioactivity of these peptides and thus we designed a 10-mer derivative with an optimised positive charge and a cyclohexylalanine (Cha) at the C-terminus for enhancing the hydrophobicity, DMPC-10A, which retained the antimicrobial activity of the parent peptide. To further investigate the influence of Cha at the C-terminus on activity, it was substituted by alanine (Ala) to generate another derivative, DMPC-10, but this was found to be much less potent. In addition, DM-PC, DMPC-19 and DMPC-10A not only rapidly killed planktonic bacteria isolated from cystic fibrosis (CF) patient, but also effectively eradicated their biofilm matrices. View Full-Text
Keywords: antimicrobial peptide; dermaseptin; peptide design; cystic fibrosis infection antimicrobial peptide; dermaseptin; peptide design; cystic fibrosis infection
Show Figures

Figure 1

MDPI and ACS Style

Ying, Y.; Wang, H.; Xi, X.; Ma, C.; Liu, Y.; Zhou, M.; Du, Q.; Burrows, J.F.; Wei, M.; Chen, T.; Wang, L. Design of N-Terminal Derivatives from a Novel Dermaseptin Exhibiting Broad-Spectrum Antimicrobial Activity against Isolates from Cystic Fibrosis Patients. Biomolecules 2019, 9, 646.

Show more citation formats Show less citations formats
Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Article Access Map by Country/Region

1
Back to TopTop