{"id":451,"date":"2013-07-22T18:18:41","date_gmt":"2013-07-22T09:18:41","guid":{"rendered":"http:\/\/120.29.164.89\/?p=451"},"modified":"2023-08-29T10:26:40","modified_gmt":"2023-08-29T01:26:40","slug":"451","status":"publish","type":"post","link":"https:\/\/www.peptide.co.jp\/en\/new-product\/451.html","title":{"rendered":"\u03b2-Defensin-3 (Human)"},"content":{"rendered":"

Novel Defensin with Broad Spectrum<\/b><\/p>\n

The human defensins represent an important family of antimicrobial peptides. They are composed of two subclasses: \u03b1-defensins such as \u03b1-defensin-1 (HNP-1, code 4271-s<\/a>) and \u03b2-defensins (hBD), which are characterized by their distinct arrangement of three disulfide bonds. Following the discovery of hBD-1 (code 4337-s<\/a>) and hBD-2 (code 4338-s<\/a>) in 1995 and 1997, respectively, hBD-3 has been included as a new member of this particular family since 2001[J. Biol. Chem.,<\/i> 276<\/b>, 5707 (2001)].<\/p>\n

\u03b2-Defensin-3 (Human):<\/b><\/p>\n

    Gly-Ile-Ile-Asn-Thr-Leu-Gln-Lys-Tyr-Tyr-Cys-Arg-Val-Arg-Gly-Gly-Arg-Cys-Ala-Val-\r\n    Leu-Ser-Cys-Leu-Pro-Lys-Glu-Glu-Gln-Ile-Gly-Lys-Cys-Ser-Thr-Arg-Gly-Arg-Lys-Cys-\r\n    Cys-Arg-Arg-Lys-Lys\r\n\r\n    (Disulfide bonds between Cys11<\/sup>-Cys40<\/sup>, Cys18<\/sup>-Cys33<\/sup>, and Cys23<\/sup>-Cys41<\/sup>)<\/pre>\n
Thus, the  hBD-3<\/a>, as well as the other defensins, are useful tools for understanding their defense mechanisms against various microorganisms.<\/p>\n\n\n\n\n
Code<\/td>\nCompound<\/td>\nPackage<\/td>\n<\/tr>\n
4382-s<\/a><\/td>\n\u03b2-Defensin-3 (Human)<\/td>\n0.1 mg vial<\/td>\n<\/tr>\n<\/tbody>\n<\/table>\n
Related Products<\/p>\n\n\n\n\n\n\n
Code<\/td>\nCompound<\/td>\nPackage<\/td>\n<\/tr>\n
4271-s<\/a><\/td>\n\u03b1-Defensin-1 (Human)<\/td>\n0.1 mg vial<\/td>\n<\/tr>\n
4337-s<\/a><\/td>\n\u03b2-Defensin-1 (Human)<\/td>\n0.1 mg vial<\/td>\n<\/tr>\n
4338-s<\/a><\/td>\n\u03b2-Defensin-2 (Human)<\/td>\n0.1 mg vial<\/td>\n<\/tr>\n<\/tbody>\n<\/table>\n","protected":false},"excerpt":{"rendered":"
Novel Defensin with Broad Spectrum<\/p>\n","protected":false},"author":1,"featured_media":0,"comment_status":"open","ping_status":"open","sticky":false,"template":"","format":"standard","meta":[],"categories":[2],"tags":[],"acf":[],"_links":{"self":[{"href":"https:\/\/www.peptide.co.jp\/en\/wp-json\/wp\/v2\/posts\/451"}],"collection":[{"href":"https:\/\/www.peptide.co.jp\/en\/wp-json\/wp\/v2\/posts"}],"about":[{"href":"https:\/\/www.peptide.co.jp\/en\/wp-json\/wp\/v2\/types\/post"}],"author":[{"embeddable":true,"href":"https:\/\/www.peptide.co.jp\/en\/wp-json\/wp\/v2\/users\/1"}],"replies":[{"embeddable":true,"href":"https:\/\/www.peptide.co.jp\/en\/wp-json\/wp\/v2\/comments?post=451"}],"version-history":[{"count":1,"href":"https:\/\/www.peptide.co.jp\/en\/wp-json\/wp\/v2\/posts\/451\/revisions"}],"predecessor-version":[{"id":4946,"href":"https:\/\/www.peptide.co.jp\/en\/wp-json\/wp\/v2\/posts\/451\/revisions\/4946"}],"wp:attachment":[{"href":"https:\/\/www.peptide.co.jp\/en\/wp-json\/wp\/v2\/media?parent=451"}],"wp:term":[{"taxonomy":"category","embeddable":true,"href":"https:\/\/www.peptide.co.jp\/en\/wp-json\/wp\/v2\/categories?post=451"},{"taxonomy":"post_tag","embeddable":true,"href":"https:\/\/www.peptide.co.jp\/en\/wp-json\/wp\/v2\/tags?post=451"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}
hBD-3<\/a> was identified in lesional psoriatic scales, from which hBD-2 was also isolated.  Peptide and DNA chemistry revealed hBD-3 to be a 45 amino acid residue peptide. The antimicrobial activity of hBD-3 is characterized by: i) a broad spectrum of antimicrobial activity against many pathogenic microbes such as multi-resistant Staphylococcus aureus<\/i> and vancomycin-resistant Enterococcus faecium<\/i> without hemolytic activity, ii) salt-insensitivity up to 200 mM NaCl, iii) expression of activity through cell wall perforation, and iv) regulation by TNF-\u03b1 and contact with bacteria[J. Biol. Chem.,<\/i> 276<\/b>, 5707 (2001)].  Later, although the data was obtained using the amino-terminally truncated peptide, hBD-3 (6-45), the following interesting findings were reported: i) hBD-3 is stimulated by interferon-\u03b3, and ii) hBD-3 has monocyte activating function and elicits ion channel activity [Cell Tissue Res.,<\/i> 306<\/b>, 257 (2001)].  It is also reported that unlike hBD-1 and hBD-2, hBD-3 mRNA expression is inhibited by corticosteroids[Biochem. Biophys. Res. Commun.,<\/i> 280<\/b>, 522 (2001)].  Significant amounts of these peptides are distributed in the following tissues: skin, tonsil, trachea, placenta, testis, thymus, and heart [J. Biol. Chem.,<\/i> 276<\/b>, 5707 (2001)], [Cell Tissue Res.,<\/i> 306<\/b>, 257 (2001)], [Gene<\/i>, 263<\/b>, 211 (2001)].  With respect to the structural aspects of hBD-3, an amphipathic dimeric structure was proposed in solution, which is different from those of hBD-1 and hBD-2.  This might be responsible for the bactericidal activity against Staphylococcus aureus<\/i>[J. Biol. Chem.,<\/i> 277<\/b>, 8279 (2002)].<\/p>\n