New Alpha-Defensin-3 and -5 Synthetic Peptides
Available
from Peptides International


Defensin peptides are effective against a wide spectrum of microbes including bacteria, viruses, fungi, spirochetes and mycobacteria.    To date, six human alpha-defensins have been classified into two sub-groups, the human neutrophil peptides (HNP) (HNP-1 to HNP-4) and the human defensins (HD), HD-5 and HD-6, which are antimicrobial peptides predominantly expressed in Paneth cells of the ileum.  Two new members of the alpha-defensin family, alpha-defensin-3 (HNP-3) (PDF-4416-s) and alpha-defensin-5 (HD-5) (PDF-4415-s), in addition to alpha-defensin-1 (HNP-1) (PDF- 4271-s), are now available to the antimicrobial research community as high purity, synthetic research tools.

            HNP-3: HNP-1 to HNP-3 are the major components of large amounts of azophilic granules of human neutrophils and are released upon neutrophil activation (1,2). The primary structures of HNP-1 to HNP-3 differ by only one amino acid residue at position 1.  HNP-2 corresponds to positions 2 through 30 of HNP-1 ([Des-Ala1]-HNP-1) while HNP-3 is [Asp1]-HNP-1.  Recent reports using HNP include: i) that HNP-1 to HNP-3 are secreted upon stimulation of CD8 cells from non-progressors of HIV-1 infection, thus, these three peptides may show anti-HIV-1 activity (3);  ii) that HNP-1 to HNP-3 are overexpressed in squamous cell carcinomas of the human tongue, representing a possible role in innate host defense against tumor invasion (4);  and iii) while expression of HNP-1 to HNP-3 is not upregulated by lipopolysaccharide (5), they locate in intestinal epithelial cells in cases of inflammatory bowel disease (6).

            HD-5: HD-5 is expressed in Paneth cells in intestinal epithelium, thus, falls into a distinct subclass of human  alpha-defensin (7,8).  In transgenic mouse models, it was confirmed that HD-5 expression was specific to Paneth cells and resulted in resistance to bacterial challenge (9). In patients with HIV-related cryptosporidiosis, HD-5 immunoreactivity was reduced in association with Paneth cell granule depletion (10).  In inflammatory bowel disease, HD-5 was expressed in metaplastic Paneth cells in the colon (6).   Based on these findings, HD-5 could be an essential factor in the defense against intestinal inflammation.  HNP-3 and HD-5, as well as HNP-1, should be valuable tools to clarify the function and mechanism of innate immunity in human beings. 

For further information about our antimicrobial products, please visit our defensins web page or contact our technical specialists today.
 

Defensin Review Articles
R.I. Lehrer and T. Ganz, Ann. N.Y. Acad. Sci., 797, 282 (1996). (Review)
M. Zasloff, Nature, 415, 389 (2002). (Review)
here
New Peptides
Product Information

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Alpha-Defensin Peptides

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PDF-4271-s

a-Defensin-1 (Human)
Alpha-Defensin-1 (Human)
HNP-1 (Human Neutrophil Peptide-1)
Ala-Cys-Tyr-Cys-Arg-Ile-Pro-Ala-Cys-Ile-Ala-Gly-Glu-Arg-Arg-Tyr-Gly-Thr-Cys-Ile-Tyr-Gln-Gly-Arg-Leu-Trp-Ala-Phe-Cys-Cys
(Disulfide bonds: Cys2-Cys30, Cys4-Cys19 and Cys9-Cys29)
M.W. 3442.1 C150H222N44O38S6
Antimicrobial Peptide / Chemoattractant for Monocyte
T. Ganz et al. J. Clin. Invest., 76, 1427 (1985).
M.E. Selsted et al. J. Clin. Invest., 76, 1436 (1985). (Original; Isolation)

0.1 mg vial

212

PDF-4416-s
NEW!

a-Defensin-3 (Human)
Alpha-Defensin-3 (Human)

HNP-3 (Human Neutrophil Peptide-3)
Asp-Cys-Tyr-Cys-Arg-Ile-Pro-Ala-Cys-Ile-Ala-Gly-Glu-Arg-Arg-Tyr-Gly-Thr-Cys-Ile-Tyr-Gln-Gly-Arg-Leu-Trp-Ala-Phe-Cys-Cys
(Disulfide bonds between Cys2-Cys30, Cys4-Cys19, and Cys9-Cys29)
(M.W. 3486.0) C151H222N44O40S6
Antimicrobial Peptide

T. Ganz, M.E. Selsted, D. Szklarek, S.S.L. Harwig, K. Daher, D.F. Bainton, and R.I. Lehrer, J. Clin. Invest., 76, 1427 (1985). (Original; Isolation)
M.E. Selsted, S.S.L. Harwig, T. Ganz, J.W. Schilling, and R.I. Lehrer, J. Clin. Invest., 76, 1436 (1985). (Original; Structure)
L. Zhang, W. Yu, T. He, J. Yu, R.E. Caffrey, E.A. Dalmasso, S. Fu, T. Pham, J. Mei, J.J. Ho, W. Zhang, P. Lopez, and D.D. Ho, Science, 298, 995 (2002).  (Pharmacol.; Anti-HIV-1 Activity)

0.1 mg vial

212

PDF-4415-s
NEW!

a-Defensin-5 (Human)
Alpha-Defensin-5 (Human)

Human Defensin-5 (HD-5)
Ala-Thr-Cys-Tyr-Cys-Arg-Thr-Gly-Arg-Cys-Ala-Thr-Arg-Glu-Ser-Leu-Ser-Gly-Val-Cys-Glu-Ile-Ser-Gly-Arg-Leu-Tyr-Arg-Leu-Cys-Cys-Arg
(Disulfide bonds between Cys3-Cys31, Cys5-Cys20, and Cys10-Cys30)
(M.W. 3582.1) C144H238N50O45S6

Antimicrobial Peptide in Paneth Cells

D.E. Jones and C.L. Bevins, J. Biol. Chem., 267, 23216 (1992).  (Original)
E. Martin Porter, M.A. Poles, J.S. Lee, J. Naitoh, C.L. Bevins, amd T. Ganz, FEBS Lett., 434, 272 (1998).  (Endogenous Form)
N.H. Salzman, D. Ghosh, K.M. Huttner, Y. Paterson, and C.L. Bevins, Nature, 422, 522 (2003).  (Pharmacol.)

0.1 mg vial

232

Article references


1) T. Ganz, M.E. Selsted, D. Szklarek, S.S.L. Harwig, K. Daher, D.F. Bainton, and R.I. Lehrer, J. Clin. Invest.,
76, 1427 (1985). (Original; Isolation of HNP 1-3)
2) M.E. Selsted, S.S.L. Harwig, T. Ganz, J.W. Schilling, and R.I. Lehrer, J. Clin. Invest., 76, 1436 (1985). (Original; Structure of HNP 1-3)
3) L. Zhang, W. Yu, T. He, J. Yu, R.E. Caffrey, E.A. Dalmasso, S. Fu, T. Pham, J. Mei, J.J. Ho, W. Zhang, P. Lopez, and D.D. Ho, Science, 298, 995 (2002).  (Pharmacol.; Anti-HIV-1 Activity)
4) F.T. Lundy, D.F. Orr, J.R. Gallagher, P. Maxwell, C. Shaw, S.S. Napier, C.G. Cowan, P.-J. Lamey, and J.J. Marley, Oral Oncol.,
40, 139 (2004).  (Pharmacol.; Role in Tumor Invasion)
5) X.-M. Fang, Q. Shu, Q.-X. Chen, M. Book, H.-G. Sahl, A. Hoeft, and F. Stuber, Eur. J. Clin. Invest., 33, 82 (2003).  (Histochem.; Regulation of Expression)
6) R.N. Cunliffe, Mol. Immunol., 40, 463 (2003).  (Histochem.;alpha-Defensin in Gastrointestinal Tract)
7) D.E. Jones and C.L. Bevins, J. Biol. Chem., 267, 23216 (1992).  (Original; Human Defensin-5)
8) E.M. Porter, M.A. Poles, J.S. Lee, J. Naitoh, C.L. Bevins, amd T. Ganz, FEBS Lett., 434, 272 (1998).  (Pharmacol.; Endogenous Form)
9) N.H. Salzman, D. Ghosh, K.M. Huttner, Y. Paterson, and C.L. Bevins, Nature, 422, 522 (2003).  (Pharmacol.)
10) P. Kelly, R. Feakins, P. Domizio, J. Murphy, C. Bevins, J. Wilson, G. Mcphail, R. Poulsom, and W. Dhaliwal, Clin. Exp. Immunol.,
135, 303 (2004).  (Histochem.; Location in AIDS Patients)

 

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