Design, Recombinant Fusion Expression and Biological Evaluation of Vasoactive Intestinal Peptide Analogue as Novel Antimicrobial Agent

Xu, Chunlan; Guo, Yu; Qiao, Xiangjin; Shang, Xiao-Ya; Niu, Weining; Jin, Mingliang

doi:10.3390/molecules22111963

Cited by 12 publications

(9 citation statements)

References 33 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The environmental pH can influence the activity and amphipathic structure of the AMPs as well as their interaction with the cell membrane of micro‐organisms (Xu et al., ). Our results also revealed pH‐dependent activity of MCH‐AMP1 (Figure b), which was seen to become stable within the narrow pH range of 7–11.…”

Section: Discussionmentioning

confidence: 99%

Isolation, functional characterization, and biological properties of MCh‐AMP1, a novel antifungal peptide from Matricaria chamomilla L.

et al. 2019

View full text Add to dashboard Cite

The antimicrobial activities of natural products have attracted much attention due to the increasing incidence of pathogens that have become resistant to drugs. Thus, it has been attempted to promisingly manage infectious diseases via a new group of therapeutic agents called antimicrobial peptides. In this study, a novel antifungal peptide, MCh‐AMP1, was purified by reverse phase HPLC and sequenced by de novo sequencing and Edman degradation. The antifungal activity, safety, thermal, and pH stability of MCh‐AMP1 were determined. This peptide demonstrated an antifungal activity against the tested Candida and Aspergillus species with MIC values in the range of 3.33–6.66 μM and 6.66–13.32 μM, respectively. Further, physicochemical properties and molecular modeling of MCh‐AMP1 were evaluated. MCh‐AMP1 demonstrated 3.65% hemolytic activity at the concentration of 13.32 μM on human red blood cells and 10% toxicity after 48 hr at the same concentration on HEK293 cell lines. The antifungal activity of MCh‐AMP1 against Candida albicans was stable at a temperature range of 30–50°C and at the pH level of 7–11. The present study indicates that MCh‐AMP1 may be considered as a new antifungal agent with therapeutic potential against major human pathogenic fungi.

show abstract

Section: Discussionmentioning

confidence: 99%

Isolation, functional characterization, and biological properties of MCh‐AMP1, a novel antifungal peptide from Matricaria chamomilla L.

et al. 2019

View full text Add to dashboard Cite

show abstract

“…However, some disadvantages limit its practical application. Therefore, in our previous research, we designed a VIP analogue, via amino residue substitution (Asp 3 →Lys 3 , Asp 8 →Lys 8 ), with safety, favorable stability and improved antimicrobial activities, and established a green, efficient and low-cost production technology via E. coli -recombinant expression system[ 21 ]. However, it remains to be elucidated whether the molecular modification and recombinant generation affect its anti-inflammatory activity or not.…”

Section: Discussionmentioning

confidence: 99%

Recombinant expressed vasoactive intestinal peptide analogue ameliorates TNBS-induced colitis in rats

Guo

Qiao

et al. 2018

WJG

Self Cite

View full text Add to dashboard Cite

AIMTo investigate the modulatory effect of recombinant-expressed vasoactive intestinal peptide (VIP) analogue (rVIPa) on trinitrobenzene sulfonic acid (TNBS)-induced colitis in rats.METHODSForty-eight rats were randomized into six groups: normal control group (Control), model control group (TNBS), ethanol treatment group (ETOH), and VIP treatment groups with different dosage (rVIPa1nmol, rVIPa2nmol, rVIPa4nmol). Diarrhea and bloody stool were observed. Colonic damage was evaluated histologically. The levels of tumor necrosis factor-α (TNF-α), interleukin-10 (IL-10), myeloperoxidase (MPO) and endotoxin in colonic tissue and serum were determined by enzyme-linked immunosorbent assay (ELISA). The expression of occludin, ZO-1, Toll-like receptor 4 (TLR4), and nuclear factor-kappa B p65 (NF-κB p65), IκBα, and p-IκBα were detected by Western blot.RESULTSAdministration with 2 nmol rVIPa prevented TNBS-induced necrosis, hyperemia, swelling, inflammation, etc., pathologic changes observed in the inner surface of colon in experimental rats. Moreover, rVIPa significantly decreased colonic TNF-α level (P < 0.001), MPO activity (P < 0.001) and serum endotoxin level (P < 0.01), and remarkably increased colonic IL-10 content (P < 0.001) in rats with TNBS-induced colitis. Furthermore, compared to the TNBS-induced colitis group, 2 nmol rVIPa treatment up-regulated the levels of occludin (P < 0.05) and ZO-1 (P < 0.05), NF-κB p65 (P < 0.01) and IκBα (P < 0.001), and down-regulated the levels of TLR4.CONCLUSIONrVIPa ameliorates TNBS-induced colonic injury and inflammation and effectively protected the intestinal mucosal barrier function in rats. The mechanism may be related to TLR4/NF-κB-mediated signaling pathway. rVIPa could be used as a new alternative therapy for intestinal inflammatory disorders.

show abstract

“…15 Furthermore, Gong et al and Xu et al reported that AMPs maintain their antimicrobial activities as fusion proteins. 16,17 Because AMPs maintain membrane activity in their fusion forms, they could be used to decorate membranes after fusion expression with proteins of interest. Ib-AMP4, which possesses two disulfide bonds, occurs in Impatiens balsamina and exhibits broad antimicrobial activity against plant pathogens.…”

Section: ■ Introductionmentioning

confidence: 88%

Using a Membrane-Penetrating-Peptide to Anchor Ligands in the Liposome Membrane Facilitates Targeted Drug Delivery

Fan

Song

et al. 2019

Bioconjugate Chem.

View full text Add to dashboard Cite

Antimicrobial peptides (AMPs) are typical cell penetrating peptides (CPPs) that intercalate into biomembranes and exhibit broad activities. We designed a triple fusion protein consisting of an AMP, Ib-AMP4 at the N-terminus, a fluorescent GFP probe in the center, and the tumor-targeting peptide P1c at the other terminus. After purification from E. coli, the interaction between the Ib-AMP4-GFP-P1c fusion protein (IGP) and the lipid membrane was characterized. Experiments using isothermal titration calorimetry (ITC) and quartz crystal microbalance with dissipation (QCM-D) demonstrated that IGP proteins spontaneously bound the lipid bilayer with a maximal molar ratio of 1:52 (protein:lipid). Furthermore, transmission electron microscopy (TEM) confirmed that the IGP protein was present in the liposome membrane. After decoration with IGP proteins, the DOPC:DOPG liposomes were applied to cancer cells. Microscopy and flow cytometry reveal that the decorated liposomes selectively bound integrin αvβ3-positive A549 cells. In addition, compared with the common chemical conjugation method, the reported method seemed to be superior in certain aspects, such as simple sample preparation and costeffectiveness. Next, the IGP protein was applied to decorate red blood cell (RBC) liposomes for targeted delivery in both in vitro and in vivo applications. The IGP-decorated RBC liposomes preferentially targeted integrin αvβ3 expressing A549 cancer cells. The in vivo imaging showed that IGP-decorated RBC liposomes were concentrated in tumor tissue and were primarily metabolized by the liver and kidney.

show abstract

Design, Recombinant Fusion Expression and Biological Evaluation of Vasoactive Intestinal Peptide Analogue as Novel Antimicrobial Agent

Cited by 12 publications

References 33 publications

Isolation, functional characterization, and biological properties of MCh‐AMP1, a novel antifungal peptide from Matricaria chamomilla L.

Isolation, functional characterization, and biological properties of MCh‐AMP1, a novel antifungal peptide from Matricaria chamomilla L.

Recombinant expressed vasoactive intestinal peptide analogue ameliorates TNBS-induced colitis in rats

Using a Membrane-Penetrating-Peptide to Anchor Ligands in the Liposome Membrane Facilitates Targeted Drug Delivery

Contact Info

Product

Resources

About