In vitro and rational design studies on structure-function of a novel bioactive peptide t-DPH1 from the skin secretion of the trigger-legged monkey tree frog, Phyllomedusa hypochondrialis

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	In vitro and rational design studies on structure-function of a novel bioactive peptide t-DPH1 from the skin secretion of the trigger-legged monkey tree frog, Phyllomedusa hypochondrialis
	Qin, H.; Ge, L.; Chen, T.; Kwok, H. F.
Source Publication	Cells
ISSN	2073-4409
Abstract	Amphibian skin derived antimicrobial peptides (AMPs) have attracted increasing attention from scientists because of their excellent bioactivity and low drug resistance. In addition to being alternative choice of antibiotics or anticancer agents, natural AMPs can also be modified as templates to further optimise their bioactivities. Here, a novel Dermaseptin peptide, t-DPH1 with extensive antimicrobial activity and antiproliferative activity, was isolated from the skin secretion of Phyllomedusa hypochondrialis through 'shotgun' cloning. To further improve the bioactivities of t-DPH1 and explore the charge threshold of enhancing bioactivity of t-DPH1, we utilised positively charged lysine residue or hydrophobic tryptophan residue to substitute one or more amino acids on the hydrophilic face of t-DPH1 the to get a series cationicity-enhanced analogue with the net charge range from +5 to +7. The present data suggest that improving the net charge could enhance the bioactivities to some extent. Still, when the charged quantity exceeds a specific limit, the bioactivities will decrease or remain the same instead of increase. When the net charge achieves the limit, improving the hydrophobicity make no sense to enhance its bioactivity. For t-DPH1, the upper limit of charged quantity is +7. All the designed analogues cationic-enhanced analogues displayed no drug resistance to gram-negative bacterial E.coli. These findings provide creative insights into the natural drug discovery and useful advice to the modification based on the novel AMPs.
Keyword	antimicrobial peptide frog skin secretion dermaseptin peptide modification
URL	View the original
Language	英語English
The Source to Article	PB_Publication
PUB ID	60433
Document Type	Journal article
Collection	DEPARTMENT OF BIOMEDICAL SCIENCES
Corresponding Author	Ge, L.; Kwok, H. F.
Recommended Citation GB/T 7714	Qin, H.,Ge, L.,Chen, T.,et al. In vitro and rational design studies on structure-function of a novel bioactive peptide t-DPH1 from the skin secretion of the trigger-legged monkey tree frog, Phyllomedusa hypochondrialis[J]. Cells.
APA	Qin, H.., Ge, L.., Chen, T.., & Kwok, H. F. In vitro and rational design studies on structure-function of a novel bioactive peptide t-DPH1 from the skin secretion of the trigger-legged monkey tree frog, Phyllomedusa hypochondrialis. Cells.
MLA	Qin, H.,et al."In vitro and rational design studies on structure-function of a novel bioactive peptide t-DPH1 from the skin secretion of the trigger-legged monkey tree frog, Phyllomedusa hypochondrialis".Cells .

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