Calorimetric Measurements of the Complexation of Cyclosporin A, Ascomycin, Fujimycin, and Rapamycin with Lithium Chloride and with an Immunophilin

Seebàch, Dieter; Bossler, Hans G.; Flowers, Robert A.; Arnett, Edward M.

doi:10.1002/hlca.19940770129

Cited by 22 publications

(8 citation statements)

References 69 publications

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“…e Values determined using ITC in [36]. f Values determined using ITC in [44]. g K i,app values determined using a PPIase enzymatic assay performed as described in [45,46].…”

Section: Generation Of a Stable Nta-his-cypa Sensor Surfacementioning

confidence: 99%

A surface plasmon resonance-based assay for small molecule inhibitors of human cyclophilin A

Wear

Patterson

Malone

et al. 2005

Analytical Biochemistry

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A simple protocol for generating a highly stable and active surface plasmon resonance (SPR) sensor surface of recombinant human hexahistidine cyclophilin A (His-CypA) is described. The sensor surface was sensitive and stable enough to allow, for the first time, the screening and ranking of several novel small-molecule (Mr approximately 250-500 Da) ligands in a competition binding assay with cyclosporin A (CsA). It also allowed us to accurately determine the kinetic rate constants for the interaction between His-CypA and CsA. His-CypA was first captured on a Ni2+-nitrilotriacetic acid (NTA) sensor chip and was then briefly covalently stabilized, coupling via primary amines. The significant baseline drift observed due to dissociation of weakly bound His-CypA from the Ni2+-NTA moiety was eliminated, resulting in a surface that was stable for at least 36 h. In addition, immobilized protein activity levels were high, typically between 85 and 95%, assayed by the interaction between His-CypA and CsA. The mean equilibrium dissociation constant for CsA (K(dCsA)) binding to the immobilized His-CypA was 23+/-6 nM, with on and off rates of 0.53+/-0.1 microM(-1) s(-1) and 1.2+/-0.1 (x 10(-2)) s(-1), respectively. These values agree well with the values for the corresponding binding constants determined from steady-state and kinetic fluorescence titrations in solution.

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“…e Values determined using ITC in [36]. f Values determined using ITC in [44]. g K i,app values determined using a PPIase enzymatic assay performed as described in [45,46].…”

Section: Generation Of a Stable Nta-his-cypa Sensor Surfacementioning

confidence: 99%

A surface plasmon resonance-based assay for small molecule inhibitors of human cyclophilin A

Wear

Patterson

Malone

et al. 2005

Analytical Biochemistry

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“…As early as 1912, Paul Pfeiffer systematically studied the crystallization of short Ala‐ and Gly‐containing peptides from aqueous solution in the presence of alkali salts1 and postulated that Li + exhibits a higher affinity (“Additionsfähigkeit”) for peptides than Na + and K + 2. Indeed, calorimetric studies revealed high interaction enthalpies for the interactions of a series of peptides with Li + ,3 values that were in the range of solvation enthalpies of peptides. These strong interactions are in practice used to increase the proportion of cis prolyl peptide bonds from 10 % to 70 % through the addition of Li salts in biochemical activity assays of peptidyl prolyl cis – trans isomerases 4.…”

Section: Introductionmentioning

confidence: 99%

How Cations Change Peptide Structure

Baldauf¹,

Pagel²,

Warnke³

et al. 2013

Chemistry A European J

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Specific interactions between cations and proteins have a strong impact on peptide and protein structure. Herein, we shed light on the nature of the underlying interactions, especially regarding effects on the polyamide backbone structure. This was done by comparing the conformational ensembles of model peptides in isolation and in the presence of either Li(+) or Na(+) by using state-of-the-art density-functional theory (including van der Waals effects) and gas-phase infrared spectroscopy. These monovalent cations have a drastic effect on the local backbone conformation of turn-forming peptides, by disruption of the hydrogen-bonding networks, thus resulting in severe distortion of the backbone conformations. In fact, Li(+) and Na(+) can even have different conformational effects on the same peptide. We also assess the predictive power of current approximate density functionals for peptide-cation systems and compare to results with those of established protein force fields as well as high-level quantum chemistry calculations (CCSD(T)).

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“…3 ) Incorporation of a cyclo-b-tetrapeptide in phospholipid bilayers induces ion conductivity [11]. 4 ) DH 0 values of up to À 37 kcal/mol have been measured [18].…”

mentioning

confidence: 99%

Preparation and NMR Structure of the Cyclo-β-tripeptide [β3-HGlu]3 in Aqueous Solution: A New Class of Enterobactin-TypeC3-Symmetrical Ligands?, Preliminary Communication

Gademann

Seebàch

1999

HCA

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Calorimetric Measurements of the Complexation of Cyclosporin A, Ascomycin, Fujimycin, and Rapamycin with Lithium Chloride and with an Immunophilin

Cited by 22 publications

References 69 publications

A surface plasmon resonance-based assay for small molecule inhibitors of human cyclophilin A

A surface plasmon resonance-based assay for small molecule inhibitors of human cyclophilin A

How Cations Change Peptide Structure

Preparation and NMR Structure of the Cyclo-β-tripeptide [β3-HGlu]3 in Aqueous Solution: A New Class of Enterobactin-TypeC3-Symmetrical Ligands?, Preliminary Communication

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