Next Article in Journal
Response of Fecal Bacterial Flora to the Exposure of Fumonisin B1 in BALB/c Mice
Previous Article in Journal
BmK86-P1, a New Degradation Peptide with Desirable Thermostability and Kv1.2 Channel-Specific Activity from Traditional Chinese Scorpion Medicinal Material
Previous Article in Special Issue
Study of Anti-Inflammatory and Analgesic Activity of Scorpion Toxins DKK-SP1/2 from Scorpion Buthus martensii Karsch (BmK)
Article

Modification Strategy of D-leucine Residue Addition on a Novel Peptide from Odorrana schmackeri, with Enhanced Bioactivity and In Vivo Efficacy

1
School of Pharmacy, Queen’s University Belfast, 97 Lisburn Road, Belfast BT9 7BL, UK
2
College of Chinese Medicinal Materials, Jilin Agricultural University, Changchun 130118, China
*
Authors to whom correspondence should be addressed.
These authors contributed equally to this work.
Received: 29 June 2021 / Revised: 20 August 2021 / Accepted: 27 August 2021 / Published: 31 August 2021
(This article belongs to the Special Issue The Frontiers of Toxin in Pharmacology)
Brevinins are a well-characterised, frog-skin-derived, antimicrobial peptide (AMP) family, but their applications are limited by high cytotoxicity. In this study, a wild-type des-Leu2 brevinin peptide, named brevinin-1OS (B1OS), was identified from Odorrana schmackeri. To explore the significant role of the leucine residue at the second position, two variants, B1OS-L and B1OS-D-L, were designed by adding L-leucine and D-leucine residues at this site, respectively. The antibacterial and anticancer activities of B1OS-L and B1OS-D-L were around ten times stronger than the parent peptide. The activity of B1OS against the growth of Gram-positive bacteria was markedly enhanced after modification. Moreover, the leucine-modified products exerted in vivo therapeutic potential in an methicillin-resistant Staphylococcus aureus (MRSA)-infected waxworm model. Notably, the single substitution of D-leucine significantly increased the killing speed on lung cancer cells, where no viable H838 cells survived after 2 h of treatment with B1OS-D-L at 10 μM with low cytotoxicity on normal cells. Overall, our study suggested that the conserved leucine residue at the second position from the N-terminus is vital for optimising the dual antibacterial and anticancer activities of B1OS and proposed B1OS-D-L as an appealing therapeutic candidate for development. View Full-Text
Keywords: brevinin; antimicrobial peptide (AMP); D-leucine peptide; cytotoxicity; dual antibacterial and anticancer activities brevinin; antimicrobial peptide (AMP); D-leucine peptide; cytotoxicity; dual antibacterial and anticancer activities
Show Figures

Figure 1

MDPI and ACS Style

Yao, A.; Ma, Y.; Chen, X.; Zhou, M.; Xi, X.; Ma, C.; Ren, S.; Chen, T.; Shaw, C.; Wang, L. Modification Strategy of D-leucine Residue Addition on a Novel Peptide from Odorrana schmackeri, with Enhanced Bioactivity and In Vivo Efficacy. Toxins 2021, 13, 611. https://0-doi-org.brum.beds.ac.uk/10.3390/toxins13090611

AMA Style

Yao A, Ma Y, Chen X, Zhou M, Xi X, Ma C, Ren S, Chen T, Shaw C, Wang L. Modification Strategy of D-leucine Residue Addition on a Novel Peptide from Odorrana schmackeri, with Enhanced Bioactivity and In Vivo Efficacy. Toxins. 2021; 13(9):611. https://0-doi-org.brum.beds.ac.uk/10.3390/toxins13090611

Chicago/Turabian Style

Yao, Aifang, Yingxue Ma, Xiaoling Chen, Mei Zhou, Xinping Xi, Chengbang Ma, Shen Ren, Tianbao Chen, Chris Shaw, and Lei Wang. 2021. "Modification Strategy of D-leucine Residue Addition on a Novel Peptide from Odorrana schmackeri, with Enhanced Bioactivity and In Vivo Efficacy" Toxins 13, no. 9: 611. https://0-doi-org.brum.beds.ac.uk/10.3390/toxins13090611

Find Other Styles
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