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Volumn 19, Issue 5, 2003, Pages 1861-1872

Adsorption of proteins to hydrophobic sites on mixed self-assembled monolayers

Author keywords

[No Author keywords available]

Indexed keywords

HYDROPHOBIC SITES;

EID: 0037418426     PISSN: 07437463     EISSN: None     Source Type: Journal    
DOI: 10.1021/la020649c     Document Type: Article
Times cited : (236)

References (68)
  • 37
    • 0345573907 scopus 로고    scopus 로고
    • note
    • The instrumental limit of detection of our BIAcore 1000 instrument is approximately 10 RU; we consider a monolayer of fibrinogen with ca. 5000 RU approximately complete.
  • 38
    • 0000170682 scopus 로고
    • Hass, G., Francombe, M., Huffman, R., Eds.; Academic Press: New York
    • Raether, H. Surface Plasma Oscillations and Their Applications; Hass, G., Francombe, M., Huffman, R., Eds.; Academic Press: New York, 1977; Vol. 9, pp 145-261.
    • (1977) Surface Plasma Oscillations and Their Applications , vol.9 , pp. 145-261
    • Raether, H.1
  • 40
    • 0344711886 scopus 로고    scopus 로고
    • note
    • Fluorescence-based techniques require the attachment of dye molecules to the proteins to enable detection; the conjugated molecular systems of dyes add significant hydrophobic character to the surface of proteins and would probably cause dye-conjugated proteins to exhibit a different adsorption isotherm with a hydrophobic surface than unfunctionalized proteins.
  • 47
    • 0345142378 scopus 로고    scopus 로고
    • note
    • The values of ΧR for which saturation is observed are approximately consistent with those calculated using the excluded volume of each R group.
  • 52
    • 15844410706 scopus 로고    scopus 로고
    • 2, but we note that the overall trend was reproducible during an independent set of experiments performed with two different batches of both alkanethiols. It is possible that the diphenyl and benzyl derivatives interact with the hydrophobic regions of the binding pocket of CA; ligands with similar structures have been found to bind effectively to CA molecules. See: Gao, J., et al. J. Med. Chem. 1996, 39, 9, 1949-1955 and Avila, L. Z., et al. J. Med. Chem. 1993, 36, 126-133. This hypothesis could potentially be verified by performing the adsorption experiments in the presence of a soluble ligand that interacts specifically with the binding pocket of CA. We have, however, not carried out these experiments.
    • (1996) J. Med. Chem. , vol.39 , Issue.9 , pp. 1949-1955
    • Gao, J.1
  • 53
    • 0027400041 scopus 로고
    • 2, but we note that the overall trend was reproducible during an independent set of experiments performed with two different batches of both alkanethiols. It is possible that the diphenyl and benzyl derivatives interact with the hydrophobic regions of the binding pocket of CA; ligands with similar structures have been found to bind effectively to CA molecules. See: Gao, J., et al. J. Med. Chem. 1996, 39, 9, 1949-1955 and Avila, L. Z., et al. J. Med. Chem. 1993, 36, 126-133. This hypothesis could potentially be verified by performing the adsorption experiments in the presence of a soluble ligand that interacts specifically with the binding pocket of CA. We have, however, not carried out these experiments.
    • (1993) J. Med. Chem. , vol.36 , pp. 126-133
    • Avila, L.Z.1
  • 54
    • 0344279923 scopus 로고    scopus 로고
    • note
    • The data of Mrksich et al. cannot be compared directly with those we report here because they were obtained with SAMs in which the hydrophobic groups were buried below the interface defined by the protruding inert groups, but they are useful in inferring the effects of the size and density of the ligand.
  • 56
    • 0345573904 scopus 로고    scopus 로고
    • note
    • 2 groups is an artifact that we cannot account for.
  • 57
    • 0000704792 scopus 로고    scopus 로고
    • Malmsten, M., Ed.; Marcel Dekker: New York
    • Tilton, R. D. Mobility of Biomolecules at Interfaces; Malmsten, M., Ed.; Marcel Dekker: New York, 1998; Vol. 75, pp 363-407.
    • (1998) Mobility of Biomolecules at Interfaces , vol.75 , pp. 363-407
    • Tilton, R.D.1
  • 59
    • 0344279922 scopus 로고    scopus 로고
    • note
    • The analysis that we carried out and the experimental data that we have gathered do not allow us to distinguish between films of adsorbed protein that are continuous or films in which individual protein molecules adsorb in discrete islands. The deviation of the measured values of ΔΦ from the predicted ones (Figure 10), however, is strong indication that the proteins do change shape on the surface.
  • 62
    • 0344711885 scopus 로고    scopus 로고
    • note
    • 2 can be used to determined the values of ΔΦ predicted by the RSA model.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.