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 L Lyubchenko, William I. Higuchi, Jindřich Kopeček

Research output: Contribution to journalArticle

66 Citations (Scopus)

Abstract

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
Volume18
Issue number5
DOIs
StatePublished - Sep 1 2007

Fingerprint

Alendronate
Skeleton
Apatites
Peptides
Bone
Durapatite
Bone and Bones
hydroxypropyl methacrylate
Apatite
Hydroxyapatite
D-Aspartic Acid
Atomic Force Microscopy
Diphosphonates
Bone Resorption
Osteogenesis
Osteoporosis
Rats
Atomic force microscopy
Copolymers
Tissue

ASJC Scopus subject areas

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

Cite this

Wang, D., Miller, S. C., Shlyakhtenko, L. S., Portillo, A. M., Liu, X. M., Papangkorn, K., ... Kopeček, J. (2007). Osteotropic peptide that differentiates functional domains of the skeleton. Bioconjugate Chemistry, 18(5), 1375-1378. https://doi.org/10.1021/bc7002132

Osteotropic peptide that differentiates functional domains of the skeleton. / Wang, Dong; Miller, Scott C.; Shlyakhtenko, Luda S.; Portillo, Alexander M.; Liu, Xin Ming; Papangkorn, Kongnara; Kopečková, Pavla; Lyubchenko, Yuri L; Higuchi, William I.; Kopeček, Jindřich.

In: Bioconjugate Chemistry, Vol. 18, No. 5, 01.09.2007, p. 1375-1378.

Research output: Contribution to journalArticle

Wang, D, Miller, SC, Shlyakhtenko, LS, Portillo, AM, Liu, XM, Papangkorn, K, Kopečková, P, Lyubchenko, YL, Higuchi, WI & Kopeček, J 2007, 'Osteotropic peptide that differentiates functional domains of the skeleton', Bioconjugate Chemistry, vol. 18, no. 5, pp. 1375-1378. https://doi.org/10.1021/bc7002132
Wang D, Miller SC, Shlyakhtenko LS, Portillo AM, Liu XM, Papangkorn K et al. Osteotropic peptide that differentiates functional domains of the skeleton. Bioconjugate Chemistry. 2007 Sep 1;18(5):1375-1378. https://doi.org/10.1021/bc7002132
Wang, Dong ; Miller, Scott C. ; Shlyakhtenko, Luda S. ; Portillo, Alexander M. ; Liu, Xin Ming ; Papangkorn, Kongnara ; Kopečková, Pavla ; Lyubchenko, Yuri L ; Higuchi, William I. ; Kopeček, Jindřich. / Osteotropic peptide that differentiates functional domains of the skeleton. In: Bioconjugate Chemistry. 2007 ; Vol. 18, No. 5. pp. 1375-1378.
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