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1. |
Making sense from antisense: A review of experimental data and developing ideas on sense–antisense peptide recognition |
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Journal of Molecular Recognition,
Volume 5,
Issue 2,
1992,
Page 43-54
Alexander Tropsha,
John S. Kizer,
Irwin M. Chaiken,
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摘要:
AbstractPeptides encoded in the antisense strand of DNA have been predicted and found experimentally to bind to sense peptides and proteins with significant selectivity and affinity. Such sense–antisense peptide recognition has been observed in many systems, most often by detecting binding between immobilized and soluble interaction partners. Data obtained so far on sequence and solvent dependence of interaction support a hydrophobic‐hydrophilic (amphipathic) model of peptide recognition. Nonetheless, the mechanistic understanding of this type of molecular recognition remains incomplete. Improving this understanding likely will require expanding the types of characteristics measured for sense–antisense peptide complexes and hence the types of analytical methods applied to such interactions. Understanding the mechanism of sense–antisense peptide recognition also may provide insights into mechanisms of native (sense) peptide and protein interactions and protein folding. Such insight may be helpful to learn how to design macromolecular recognition agents in technology for separation, diagnostics and thera
ISSN:0952-3499
DOI:10.1002/jmr.300050202
出版商:John Wiley&Sons, Ltd.
年代:1992
数据来源: WILEY
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2. |
Design of novel affinity adsorbents for the purification of trypsin‐like proteases |
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Journal of Molecular Recognition,
Volume 5,
Issue 2,
1992,
Page 55-68
Nicolas P. Burton,
Christopher R. Lowe,
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摘要:
AbstractA number of ligands for the selective purification by affinity chromatography of the trypsin‐like protease, porcine pancreatic kallikrein, were designedde novoby computer‐aided molecular design. The ligands were designed to mimic the side‐chains of a number of arginyl dipeptides and included a benzamidine moiety substituted on a triazine ring. The ligands displayed inhibitory activities against pancreatic kallikrein which mirrored the specificity constants of the dipeptides they were designed to mimic. The ligand with the highest affinity for the enzyme, and analogue of a Phe‐Arg dipeptide, when immobilized to Sepharose CL‐4B via a hexamethylene spacer arm, purified pancreatic kallikrein 110‐fold in one step from a crude pancreatic acet
ISSN:0952-3499
DOI:10.1002/jmr.300050203
出版商:John Wiley&Sons, Ltd.
年代:1992
数据来源: WILEY
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3. |
Complex carbohydrate–lectin interaction at the interface: a model for cellular adhesion. II. Reactivity of both the oligosaccharide chain and sugar‐binding domain of a glycoprotein lectin |
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Journal of Molecular Recognition,
Volume 5,
Issue 2,
1992,
Page 69-73
Abhijit Chakrabarti,
Sunil K. Podder,
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摘要:
AbstractWe describe studies of a new model cell adhesion system involving liposomes bearing lectins and the glycosphingolipid, asialomonosialoganglioside (asialoGM1). The model provides a simple analysis of experimental data to elucidate the mechanism of heterophilic cell–cell adhesion mediated by multiple protein–carbohydrate interactions. Phospholipid vesicles bearing the fatty acid conjugate of a glycoprotein lectin fromRicinus communis(RCAI vesicle) are shown to react with vesicles bearing the fatty acid conjugate of Concanavalin A (Con A) and asialoGM1(Con A vesicle). The kinetics of aggregation and monosaccharide‐induced disaggregation of the two types of vesicles were followed by monitoring the time‐dependent change in turbidity. Depending on the surface density of the asialoGM1, 40–60% of the resulting precipitin complex was dissociable only in the presence of both RCAI‐specific galactose and Con A‐specific α‐methyl‐D‐mannoside. Results indicate simultaneous participation of both the saccharide‐binding domain and carbohydrage sequence of RCAI, a model cell adhesion molecule, to stabilize the encounter complex by two types of interactions. These findings support the possibility of stable cell–cell adhesionin vivooccurring via interactions between cell adhesion molecules on apposin
ISSN:0952-3499
DOI:10.1002/jmr.300050204
出版商:John Wiley&Sons, Ltd.
年代:1992
数据来源: WILEY
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4. |
Quantitative structure–activity relationship studies on benzodiazepine receptor binding: Recognition of active sites in receptor and modelling of interaction |
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Journal of Molecular Recognition,
Volume 5,
Issue 2,
1992,
Page 75-80
Satya P. Gupta,
Ranendra N. Saha,
Veena Mulchandani,
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摘要:
AbstractA quantitative structure‐activity relationship study was carried out for the binding of a series of ‘classical’ benzodiazepines (BZs) and some β‐carbolines with BZ receptors to investigate the active sites in the latter and the nature of the binding of compounds with them. Using the Hansch approach, an attempt was made to correlate binding affinities of compounds with various physico‐chemical and electronic properties of substituents. The correlations obtained showed the main roles were played by the hydrophobic constant π and the Hammett constant σ (an electronic parameter) of various substituents. This led to the suggestion that BZ receptors have many additional hydrophobic, hydrogen bonding and polor sites other than those suggested by Hollinsheadet al.(1990). From the present study, the Hollinshead model of interaction was found to be inadequate to account fully for the binding of all types
ISSN:0952-3499
DOI:10.1002/jmr.300050205
出版商:John Wiley&Sons, Ltd.
年代:1992
数据来源: WILEY
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5. |
Erratum |
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Journal of Molecular Recognition,
Volume 5,
Issue 2,
1992,
Page 81-81
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ISSN:0952-3499
DOI:10.1002/jmr.300050206
出版商:John Wiley&Sons, Ltd.
年代:1992
数据来源: WILEY
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6. |
Masthead |
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Journal of Molecular Recognition,
Volume 5,
Issue 2,
1992,
Page -
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PDF (97KB)
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ISSN:0952-3499
DOI:10.1002/jmr.300050201
出版商:John Wiley&Sons, Ltd.
年代:1992
数据来源: WILEY
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