Next Article in Journal
Synthesis, Screening and Pharmacokinetic Evaluation of Potential Prodrugs of Bupropion. Part One: In Vitro Development
Next Article in Special Issue
Antimicrobial Peptides in Reptiles
Previous Article in Journal
Barriers to the Access and Use of Rituximab in Patients with Non-Hodgkin’s Lymphoma and Chronic Lymphocytic Leukemia: A Physician Survey
Previous Article in Special Issue
“Specificity Determinants” Improve Therapeutic Indices of Two Antimicrobial Peptides Piscidin 1 and Dermaseptin S4 Against the Gram-negative Pathogens Acinetobacter baumannii and Pseudomonas aeruginosa

Human Antimicrobial Peptides and Proteins

Department of Pathology and Microbiology, College of Medicine, University of Nebraska Medical Center, 986495 Nebraska Medical Center, Omaha, NE 68198-6495, USA
Pharmaceuticals 2014, 7(5), 545-594;
Received: 17 January 2014 / Revised: 15 April 2014 / Accepted: 29 April 2014 / Published: 13 May 2014
As the key components of innate immunity, human host defense antimicrobial peptides and proteins (AMPs) play a critical role in warding off invading microbial pathogens. In addition, AMPs can possess other biological functions such as apoptosis, wound healing, and immune modulation. This article provides an overview on the identification, activity, 3D structure, and mechanism of action of human AMPs selected from the antimicrobial peptide database. Over 100 such peptides have been identified from a variety of tissues and epithelial surfaces, including skin, eyes, ears, mouths, gut, immune, nervous and urinary systems. These peptides vary from 10 to 150 amino acids with a net charge between −3 and +20 and a hydrophobic content below 60%. The sequence diversity enables human AMPs to adopt various 3D structures and to attack pathogens by different mechanisms. While α-defensin HD-6 can self-assemble on the bacterial surface into nanonets to entangle bacteria, both HNP-1 and β-defensin hBD-3 are able to block cell wall biosynthesis by binding to lipid II. Lysozyme is well-characterized to cleave bacterial cell wall polysaccharides but can also kill bacteria by a non-catalytic mechanism. The two hydrophobic domains in the long amphipathic α-helix of human cathelicidin LL-37 lays the basis for binding and disrupting the curved anionic bacterial membrane surfaces by forming pores or via the carpet model. Furthermore, dermcidin may serve as ion channel by forming a long helix-bundle structure. In addition, the C-type lectin RegIIIα can initially recognize bacterial peptidoglycans followed by pore formation in the membrane. Finally, histatin 5 and GAPDH(2-32) can enter microbial cells to exert their effects. It appears that granulysin enters cells and kills intracellular pathogens with the aid of pore-forming perforin. This arsenal of human defense proteins not only keeps us healthy but also inspires the development of a new generation of personalized medicine to combat drug-resistant superbugs, fungi, viruses, parasites, or cancer. Alternatively, multiple factors (e.g., albumin, arginine, butyrate, calcium, cyclic AMP, isoleucine, short-chain fatty acids, UV B light, vitamin D, and zinc) are able to induce the expression of antimicrobial peptides, opening new avenues to the development of anti-infectious drugs. View Full-Text
Keywords: antimicrobial chemokines; antimicrobial neuropeptides; antimicrobial proteins; cathelicidin LL-37; defensins; dermcidin; hepcidins; histatins; RNases antimicrobial chemokines; antimicrobial neuropeptides; antimicrobial proteins; cathelicidin LL-37; defensins; dermcidin; hepcidins; histatins; RNases
Show Figures

Figure 1

MDPI and ACS Style

Wang, G. Human Antimicrobial Peptides and Proteins. Pharmaceuticals 2014, 7, 545-594.

AMA Style

Wang G. Human Antimicrobial Peptides and Proteins. Pharmaceuticals. 2014; 7(5):545-594.

Chicago/Turabian Style

Wang, Guangshun. 2014. "Human Antimicrobial Peptides and Proteins" Pharmaceuticals 7, no. 5: 545-594.

Find Other Styles

Article Access Map by Country/Region

Only visits after 24 November 2015 are recorded.
Back to TopTop