Osteotropic Peptide That Differentiates Functional Domains of the Skeleton

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• 作者：Dong Wang ; Scott C. Miller ; Luda S. Shlyakhtenko ; Alexander M. Portillo ; Xin-Ming Liu ; Kongnara Papangkorn ; Pavla Kopeková ; Yuri Lyubchenko ; William I. Higuchi ; Jindich Kopeek
• 刊名：Bioconjugate Chemistry
• 出版年：2007
• 出版时间：September 2007
• 年：2007
• 卷：18
• 期：5
• 页码：1375 - 1378
• 全文大小：250K
• 年卷期：v.18,no.5(September 2007)
• ISSN：1520-4812

文摘

HPMA copolymer-D-aspartic acid octapeptide (D-Asp₈) conjugates have been found to target the entire skeletonafter systemic administration. In a recent study using the ovariectomized rat model of osteoporosis, we surprisinglydiscovered that D-Asp₈ would favorably recognize resorption sites in skeletal tissues, while another bone-targetingmoiety, alendronate (ALN), directs the delivery system to both formation and resorption sites. Atomic forcemicroscopy (AFM) analyses reveal that ALN has a stronger binding force to hydroxyapatite (HA) than D-Asp₈.In vitro HA binding studies indicate that D-Asp₈ is more sensitive to change of HA crystallinity than ALN.Because the bone apatite in the newly formed bone (formation sites) usually has lower crystallinity than theresorption sites (mainly mature bone), we believe that the favorable recognition of D-Asp₈ to the bone resorptionsites could be attributed to its relatively weak binding to apatite, when compared to bisphosphonates, and thedifferent levels of crystallinity of bone apatite at different functional domains of the skeleton.