Beta-Defensin-3 (Human)
hBD-3 | Human β-Defensin-3

4382-s 0.1 mg | 235.00 EUR

Synthetic Product (disulfide bonds between Cys¹¹-Cys⁴⁰, Cys¹⁸-Cys³³ and Cys²³-Cys⁴¹)

Gly - Ile - Ile - Asn - Thr - Leu - Gln - Lys - Tyr - Tyr - Cys - Arg - Val - Arg - Gly - Gly - Arg - Cys - Ala - Val - Leu - Ser - Cys - Leu - Pro - Lys - Glu - Glu - Gln - Ile - Gly - Lys - Cys - Ser - Thr - Arg - Gly - Arg - Lys - Cys - Cys - Arg - Arg - Lys - Lys

(M.W. 5155.1)

C216H371N75O59S6

The purity of Human Beta-Defensin-3 is guaranteed to be higher than 99% by HPLC

Download PDF-data-sheet:

Antimicrobial Peptide / Staphylococcus aureus-Killing Factor

The human defensin peptides represent a new and important family of antimicrobial peptides. The defensin peptides are grouped in two subfamilies, the alpha-Defensins such as human alpha-defensin-1 (HNP-1, Code 4271-s) and the beta-Defensin (hBD) family.
The discovery of two new antimicrobial peptides described as human beta-defensin-1 (hBD-1, Code 4337-s) and human beta-defensin-2 hBD-2, Code 4338-s) was followed by the description of Human Beta-Defensin-3.
HBD-3 was identified in skin of psoriac disease patients, from which hBD-2 was also isolated. Beta-Defensin-3 was described by peptide chemical methods as a polypeptide composed of 45 amino acid residues and three distinct disulfide bridges.

The antimicrobial activity of hBD-3 is characterised by:

1. a broad spectrum of antimicrobial activity against many pathogenic microbes such as multi resistant Staphylococcus aureus and vancomycin-resistant Enterococcus faecium without hemolytic activity,
2. salt-intesnity up to 200nM NaCl,
3. expression of activity through cell wall perforation, and
4. regulation of TNF-α and contact with bacteria.

In solution, an amphipatic dimeric structure was assumed for hBD-3. This is quite different from the proposed structures of hBD-1 and hBD-2. This different structure of hBD-3 compared to those of hBD-1 and hBD-2 might be the reason for the differences in the bacterial activity against Staphylococcus aureus.

References:

1. T. Harder, J. Bartels, E. Christophers and J.M. Schröder, J. Biol. Chem., 276, 5707 (2001) (Original description of beta-defensin-3)
2. J.R.C. Garcia, F. Jaumann, S. Schulz, A. KrauseJ. Rodringuez-Jiménez, U. Forssmann, K. Adermann, E. Klüver, C. Vogelmeier, D. Becker, R. Hedrich, W.G. Forssmann and R. Bals, Cell. Tissue. Res., 306, 257 (2001) (Original; Amino-Terminally Truncated Peptide)
3. L.A. Duits, M. Rademaker, B. Ravensberger, M.A.J.A. van Sterkenburg, E. van Strijen, P.S. Hiemstra and P.H. Nibbering, Biochem. Biophys. Res. Commun., 280, 522 (2001) (Pharmacology)
4. H.P.Ija, B.C. Schutte, A. Schudy, R. Linzmeier, J.M. Guthmiller, G.K. Johnson, B.F. Tack, J.P. Mitros, A. Rosenthal, T. Ganz and P.B. McCray, Jr., Gene, 263, 211 (2001) (DNA Sequenz / Tissue Distribution)
5. D.J Schibli, H.N. Hunter, V. Aseyev, T.D. Starner, J.M. Wiencek, P.B. McCray, Jr., B.F. Tack, and H.J. Vogel, J. Biol. Chem., 277, 8279 (2002) (Solution Structure of hBD-3)

Links to publications that use our peptide beta-Defensin-3 | code 4382-s:

1. β-Defensins chemoattract macrophages and mast cells but not lymphocytes and dendritic cells: CCR6 is not involved
2. Differential activity of innate defense antimicrobial peptides against Nocardia species