Osteotropic peptide that differentiates functional domains of the skeleton

Dong Wang, Scott C. Miller, Luda S. Shlyakhtenko, Alexander M. Portillo, Xin Ming Liu, Kongnara Papangkorn, Pavla Kopečková, Yuri Lyubchenko, William I. Higuchi, Jindřich Kopeček

Research output: Contribution to journalArticlepeer-review

99 Scopus citations


HPMA copolymer - D-aspartic acid octapeptide (D-Asp8) conjugates have been found to target the entire skeleton after systemic administration. In a recent study using the ovariectomized rat model of osteoporosis, we surprisingly discovered that D-Asp8 would favorably recognize resorption sites in skeletal tissues, while another bone-targeting moiety, alendronate (ALN), directs the delivery system to both formation and resorption sites. Atomic force microscopy (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 the resorption sites (mainly mature bone), we believe that the favorable recognition of D-Asp 8 to the bone resorption sites could be attributed to its relatively weak binding to apatite, when compared to bisphosphonates, and the different levels of crystallinity of bone apatite at different functional domains of the skeleton.

Original languageEnglish (US)
Pages (from-to)1375-1378
Number of pages4
JournalBioconjugate Chemistry
Issue number5
StatePublished - 2007

ASJC Scopus subject areas

  • Biotechnology
  • Bioengineering
  • Biomedical Engineering
  • Pharmacology
  • Pharmaceutical Science
  • Organic Chemistry


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