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Biomedicines
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Antimicrobial Peptides Aka Host Defense Peptides – from Basic Research...
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Antimicrobial Peptides Aka Host Defense Peptides – from Basic Research to Therapy 2.0

A special issue of Biomedicines (ISSN 2227-9059). This special issue belongs to the section "Molecular and Translational Medicine".

Deadline for manuscript submissions: closed (15 December 2022) | Viewed by 4595

Special Issue Editor

Dr. Jitka Petrlova

E-Mail Website
Guest Editor
Department of Clinical Sciences, Division of Dermatology and Venereology, Lund University, Lund, Sweden
Interests: peptide; inflammatory; aggregation; apolipoprotiens; innate immunity; host defense peptides
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

All wounds are at risk of becoming contaminated by pathogens, which could lead to infection. The ability to effectively overcome this danger is of evolutionary significance to our survival. It is therefore not surprising that multiple host defense systems, such as host defense peptides, have evolved. Antimicrobial peptides, aka host-defense peptides (HDPs), are produced by all living organisms, including bacteria, fungi, plants, invertebrates, and vertebrates. These peptides display activity against bacteria, fungi, viruses, and parasites. Today we have clear evidence that HDPs have far more than broad-spectrum antimicrobial activity, including immunomodulatory effects, wound healing, LPS neutralization, chemotaxis, or anti-cancer effects. Moreover, the multifunctionality of HDPs puts a lot of interest in the development of new therapeutic strategies against infectious diseases.

This Special Issue will address the most current and innovative developments in the field of HDPs research with a range of topics such as structure and function analysis, modes of action, anti-microbial effects, cell and animal model systems, the discovery of novel host defense peptides, and drug development.

Dr. Jitka Petrlova
Guest Editor

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Biomedicines is an international peer-reviewed open access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2600 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • antimicrobial peptides
  • host defense peptides
  • innate immunity
  • wound healing

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Published Papers (2 papers)

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Research

15 pages, 1796 KiB  
Article
Transforming Cross-Linked Cyclic Dimers of KR-12 into Stable and Potent Antimicrobial Drug Leads
by Taj Muhammad, Adam A. Strömstedt, Sunithi Gunasekera and Ulf Göransson
Biomedicines 2023, 11(2), 504; https://doi.org/10.3390/biomedicines11020504 - 9 Feb 2023
Cited by 8 | Viewed by 2294
Abstract
Is it possible to enhance structural stability and biological activity of KR-12, a truncated antimicrobial peptide derived from the human host defense peptide LL-37? Based on the mapping of essential residues in KR-12, we have designed backbone-cyclized dimers, cross-linked via a disulfide bond [...] Read more.
Is it possible to enhance structural stability and biological activity of KR-12, a truncated antimicrobial peptide derived from the human host defense peptide LL-37? Based on the mapping of essential residues in KR-12, we have designed backbone-cyclized dimers, cross-linked via a disulfide bond to improve peptide stability, while at the same time improving on-target activity. Circular dichroism showed that each of the dimers adopts a primarily alpha-helical conformation (55% helical content) when bound to lyso-phosphatidylglycerol micelles, indicating that the helical propensity of the parent peptide is maintained in the new cross-linked cyclic form. Compared to KR-12, one of the cross-linked dimers showed 16-fold more potent antimicrobial activity against human pathogens Pseudomonas aeruginosa, Staphylococcus aureus, and Candida albicans and 8-fold increased activity against Escherichia coli. Furthermore, these peptides retained antimicrobial activity at physiologically relevant conditions, including in the presence of salts and in human serum, and with selective Gram-negative antibacterial activity in rich growth media. In addition to giving further insight into the structure–activity relationship of KR-12, the current work demonstrates that by combining peptide stabilization strategies (dimerization, backbone cyclization, and cross-linking via a disulfide bond), KR-12 can be engineered into a potent antimicrobial peptide drug lead with potential utility in a therapeutic context. Full article
(This article belongs to the Special Issue Antimicrobial Peptides Aka Host Defense Peptides – from Basic Research to Therapy 2.0)
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11 pages, 1124 KiB  
Article
Clinical Significance of Serum Elafin in Children with Inflammatory Bowel Disease
by Paulina Krawiec and Elżbieta Pac-Kożuchowska
Biomedicines 2022, 10(12), 3267; https://doi.org/10.3390/biomedicines10123267 - 16 Dec 2022
Cited by 4 | Viewed by 1727
Abstract
Background: The role of elafin in the pathophysiology of inflammatory bowel disease (IBD) has not been not elucidated. We aimed to evaluate serum elafin in children with IBD and assess its relationship with disease activity. Methods: We enrolled children with IBD in the [...] Read more.
Background: The role of elafin in the pathophysiology of inflammatory bowel disease (IBD) has not been not elucidated. We aimed to evaluate serum elafin in children with IBD and assess its relationship with disease activity. Methods: We enrolled children with IBD in the study group and children with functional abdominal pain in the control group. We evaluated serum elafin using enzyme-linked immunosorbent assay kits. Results: In children with IBD, serum elafin (mean ± SD: 4.192 ± 1.424 ng/mL) was significantly elevated compared with controls (mean ± SD: 3.029 ± 1.366 ng/mL) (p = 0.0005). Elafin was significantly increased in children in the active phase of IBD (mean ± SD: 4.424 ± 1.449 ng/mL) compared with the control group (p = 0.0003). In IBD remission, only children with ulcerative colitis (mean ± SD: 4.054 ± 1.536 ng/mL) had elevated elafin compared with controls (p = 0.004). ROC analysis revealed that the area under the curve (AUC) of serum elafin was 0.809 while discriminating patients with ulcerative colitis from the control group, and the AUC was 0.664 while differentiating patients with Crohn’s disease from the control group. Conclusions: Serum elafin was found to be elevated in our cohort of children with IBD, depending on disease activity. Serum elafin was increased in the active phases of both ulcerative colitis and Crohn’s disease, but only in the remission of ulcerative colitis. Elafin appears to be a potential candidate for a biomarker of ulcerative colitis. Full article
(This article belongs to the Special Issue Antimicrobial Peptides Aka Host Defense Peptides – from Basic Research to Therapy 2.0)
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