Thermodynamic analysis of the drug-receptor interaction

Robert B. Raffa, Frank Porreca

Research output: Contribution to journalArticle

51 Citations (Scopus)

Abstract

Thermodynamic analysis of pharmacologic data potentially offers an insight into the molecular events underlying drug-receptor interactions not obtainable by other techniques. Embodied in thermodynamics are the laws governing the interconvertibility of heat and work and, hence, it is a particularly apt framework for the analysis of the transduction of information from ligand to biological tissue during the initiation of a drug effect. Implicit in thermodynamic analysis of pharmacologic data is quantitative measurement of the driving forces involved in the drug-receptor interaction (in place of less precise terms such as "affinity"). In addition, the cautious interpretation of thermodynamic analysis can give clues to the underlying mechanisms of the drug-receptor interaction that is beyond the resolving power of other parameters, such as the dissociation constant. The present review is an attempt to identify repsresentative reports that have overtly analyzed pharmacologic data with thermodynamic analysis, to summarize the findings within and across studies (particularly regarding enthapy - versus entropy-driven binding of agonists and antagonists), to point out and address some apparent inconsistencies that can arise, and to consider the application of thermodynamic analysis to data obtained using isolated tissue preparations.

Original languageEnglish (US)
Pages (from-to)245-258
Number of pages14
JournalLife Sciences
Volume44
Issue number4
DOIs
StatePublished - 1989

Fingerprint

Drug Receptors
Drug Interactions
Thermodynamics
Tissue
Optical resolving power
Entropy
Hot Temperature
Ligands
Pharmaceutical Preparations

ASJC Scopus subject areas

  • Pharmacology

Cite this

Thermodynamic analysis of the drug-receptor interaction. / Raffa, Robert B.; Porreca, Frank.

In: Life Sciences, Vol. 44, No. 4, 1989, p. 245-258.

Research output: Contribution to journalArticle

Raffa, Robert B. ; Porreca, Frank. / Thermodynamic analysis of the drug-receptor interaction. In: Life Sciences. 1989 ; Vol. 44, No. 4. pp. 245-258.
@article{8f0825a6d65e4e43b677bdab2cf12c13,
title = "Thermodynamic analysis of the drug-receptor interaction",
abstract = "Thermodynamic analysis of pharmacologic data potentially offers an insight into the molecular events underlying drug-receptor interactions not obtainable by other techniques. Embodied in thermodynamics are the laws governing the interconvertibility of heat and work and, hence, it is a particularly apt framework for the analysis of the transduction of information from ligand to biological tissue during the initiation of a drug effect. Implicit in thermodynamic analysis of pharmacologic data is quantitative measurement of the driving forces involved in the drug-receptor interaction (in place of less precise terms such as {"}affinity{"}). In addition, the cautious interpretation of thermodynamic analysis can give clues to the underlying mechanisms of the drug-receptor interaction that is beyond the resolving power of other parameters, such as the dissociation constant. The present review is an attempt to identify repsresentative reports that have overtly analyzed pharmacologic data with thermodynamic analysis, to summarize the findings within and across studies (particularly regarding enthapy - versus entropy-driven binding of agonists and antagonists), to point out and address some apparent inconsistencies that can arise, and to consider the application of thermodynamic analysis to data obtained using isolated tissue preparations.",
author = "Raffa, {Robert B.} and Frank Porreca",
year = "1989",
doi = "10.1016/0024-3205(89)90182-3",
language = "English (US)",
volume = "44",
pages = "245--258",
journal = "Life Sciences",
issn = "0024-3205",
publisher = "Elsevier Inc.",
number = "4",

}

TY - JOUR

T1 - Thermodynamic analysis of the drug-receptor interaction

AU - Raffa, Robert B.

AU - Porreca, Frank

PY - 1989

Y1 - 1989

N2 - Thermodynamic analysis of pharmacologic data potentially offers an insight into the molecular events underlying drug-receptor interactions not obtainable by other techniques. Embodied in thermodynamics are the laws governing the interconvertibility of heat and work and, hence, it is a particularly apt framework for the analysis of the transduction of information from ligand to biological tissue during the initiation of a drug effect. Implicit in thermodynamic analysis of pharmacologic data is quantitative measurement of the driving forces involved in the drug-receptor interaction (in place of less precise terms such as "affinity"). In addition, the cautious interpretation of thermodynamic analysis can give clues to the underlying mechanisms of the drug-receptor interaction that is beyond the resolving power of other parameters, such as the dissociation constant. The present review is an attempt to identify repsresentative reports that have overtly analyzed pharmacologic data with thermodynamic analysis, to summarize the findings within and across studies (particularly regarding enthapy - versus entropy-driven binding of agonists and antagonists), to point out and address some apparent inconsistencies that can arise, and to consider the application of thermodynamic analysis to data obtained using isolated tissue preparations.

AB - Thermodynamic analysis of pharmacologic data potentially offers an insight into the molecular events underlying drug-receptor interactions not obtainable by other techniques. Embodied in thermodynamics are the laws governing the interconvertibility of heat and work and, hence, it is a particularly apt framework for the analysis of the transduction of information from ligand to biological tissue during the initiation of a drug effect. Implicit in thermodynamic analysis of pharmacologic data is quantitative measurement of the driving forces involved in the drug-receptor interaction (in place of less precise terms such as "affinity"). In addition, the cautious interpretation of thermodynamic analysis can give clues to the underlying mechanisms of the drug-receptor interaction that is beyond the resolving power of other parameters, such as the dissociation constant. The present review is an attempt to identify repsresentative reports that have overtly analyzed pharmacologic data with thermodynamic analysis, to summarize the findings within and across studies (particularly regarding enthapy - versus entropy-driven binding of agonists and antagonists), to point out and address some apparent inconsistencies that can arise, and to consider the application of thermodynamic analysis to data obtained using isolated tissue preparations.

UR - http://www.scopus.com/inward/record.url?scp=0024496899&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0024496899&partnerID=8YFLogxK

U2 - 10.1016/0024-3205(89)90182-3

DO - 10.1016/0024-3205(89)90182-3

M3 - Article

C2 - 2536880

AN - SCOPUS:0024496899

VL - 44

SP - 245

EP - 258

JO - Life Sciences

JF - Life Sciences

SN - 0024-3205

IS - 4

ER -