Kinetics of the interaction of desAABB–fibrin monomer with immobilized fibrinogen

Chtcheglova, Lilia A.; Vogel, Monique; Gruber, Hermann J.; Dietler, Giovanni; Haeberli, André

doi:10.1002/bip.20529

Cited by 11 publications

(5 citation statements)

References 56 publications

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“…These affinities are somewhat weaker than the affinities we determined for the larger desA‐ and desAB‐NDSK fragments, which likely reflects the entropy costs associated with restraining the conformations of the smaller molecules. Considered with the published data [19,38,40,41], the values we determined by SPR are rational, indicating that our data reflect the affinities of the ‘A‐a’ and ‘B‐b’ interactions as they occur in fibrin polymers.…”

Section: Discussionsupporting

confidence: 78%

“…These affinities are somewhat weaker than the affinities we determined for the larger desA-and desAB-NDSK fragments, which likely reflects the entropy costs associated with Fibrin Ôknob-holeÕ interactions 2349 restraining the conformations of the smaller molecules. Considered with the published data [19,38,40,41], the values we determined by SPR are rational, indicating that our data reflect the affinities of the ÔA-aÕ and ÔB-bÕ interactions as they occur in fibrin polymers. The observation that desAB-NDSK binds fibrinogen through both ÔA-aÕ and ÔB-bÕ interactions infers that both sets of interactions can occur between the same two fibrin molecules in a polymer.…”

Section: Discussionsupporting

confidence: 76%

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Role of ‘B‐b’ knob‐hole interactions in fibrin binding to adsorbed fibrinogen

Geer

Tripathy

Lord

et al. 2007

Journal of Thrombosis and Haemostasis

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Summary. Background: The formation of a fibrin clot is supported by multiple interactions, including those between polymerization knobs ÔAÕ and ÔBÕ exposed by thrombin cleavage and polymerization holes ÔaÕ and ÔbÕ present in fibrinogen and fibrin. Although structural studies have defined the ÔA-aÕ and ÔB-bÕ interactions in part, it has not been possible to measure the affinities of individual knob-hole interactions in the absence of the other interactions occurring in fibrin. Objectives: We designed experiments to determine the affinities of knob-hole interactions, either ÔA-aÕ alone or ÔA-aÕ and ÔB-bÕ together. Methods: We used surface plasmon resonance to measure binding between adsorbed fibrinogen and soluble fibrin fragments containing ÔAÕ knobs, desA-NDSK, or both ÔAÕ and ÔBÕ knobs, desAB-NDSK. Results: The desA-and desAB-NDSK fragments bound to fibrinogen with statistically similar K d Õs of 5.8 ± 1.1 lM and 3.7 ± 0.7 lM (P = 0.14), respectively. This binding was specific, as we saw no significant binding of NDSK, which has no exposed knobs. Moreover, the synthetic ÔAÕ knob peptide GPRP and synthetic ÔBÕ knob peptides GHRP and AHRPY, inhibited the binding of desA-and/or desAB-NDSK. Conclusions: The peptide inhibition findings show both ÔA-aÕ and ÔB-bÕ interactions participate in desAB-NDSK binding to fibrinogen, indicating ÔB-bÕ interactions can occur simultaneously with ÔA-aÕ. Furthermore, ÔA-aÕ interactions are much stronger than ÔB-bÕ because the affinity of desA-NDSK was not markedly different from desAB-NDSK.

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Section: Discussionsupporting

confidence: 78%

Section: Discussionsupporting

confidence: 76%

Role of ‘B‐b’ knob‐hole interactions in fibrin binding to adsorbed fibrinogen

Geer

Tripathy

Lord

et al. 2007

Journal of Thrombosis and Haemostasis

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“…The interaction between fibrin monomers and fibrin(ogen), or vice versa, is characterized by a rather high affinity (K D of ϳ 10 Ϫ8 M) and a change of standard Gibbs energy of approximately Ϫ10 kcal/mol. 36 These data demonstrate that the equilibrium is thermodynamically favored for the formation of a stable fibrin-fibrinogen complex. We have shown previously that the overall structure of fibrin arising with the preferential release of FpB by a specific snake venom enzyme is essentially the same as the structure of fibrin initiated by thrombin.…”

Section: Fibrinopeptide Release From Surface Fibrin 1703mentioning

confidence: 80%

Fibrinopeptides A and B release in the process of surface fibrin formation

Riedel

Suttnar

Brynda

et al. 2011

Blood

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Fibrinogen adsorption on a surface results in the modification of its functional characteristics. Our previous studies revealed that fibrinogen adsorbs onto surfaces essentially in 2 different orientations depending on its concentration in the solution: "side-on" at low concentrations and "end-on" at high concentrations. In the present study, we analyzed the thrombin-mediated release of fibrinopeptides A and B (FpA and FpB) from fibrinogen adsorbed in these orientations, as well as from surface-bound fibrinogenfibrin complexes prepared by converting fibrinogen adsorbed in either orientation into fibrin and subsequently adding fibrinogen. The release of fibrinopeptides from surface-adsorbed fibrinogen and from surface-bound fibrinogen-fibrin complexes differed significantly compared with that from fibrinogen in solution. The release of FpB occurred without the delay (lag phase) characteristic of its release from fibrinogen in solution. The amount of FpB released from end-on adsorbed fibrinogen and from adsorbed fibrinogenfibrin complexes was much higher than that of FpA. FpB is known as a potent chemoattractant, so its preferential release suggests a physiological purpose in the attraction of cells to the site of injury. The N-terminal portions of fibrin ␤ chains including residues B␤15-42, which are exposed after cleavage of FpB, have been implicated in many processes, including angiogenesis and inflammation. (Blood. 2011;117(5):1700-1706) IntroductionFibrinogen, one of the most abundant proteins in blood, plays a key role in hemostasis, inflammation, wound healing, and additional physiological and pathological processes. Immediately after blood comes in contact with artificial materials or with an injured vessel wall subendothelium, fibrinogen rapidly adsorbs on the surface and interacts with adhered activated platelets and subendothelial proteins. Numerous studies have demonstrated that fibrinogen in solution and fibrinogen adsorbed on various surfaces exhibit different properties. [1][2][3][4] For example, surface-adsorbed fibrinogen changes its conformation and thus reveals multiple binding sites that interact with the receptors on platelets and leukocytes. 5,6 These reciprocal interactions participate in the process of blood clot formation and in the inflammatory response. Platelet adhesion promoted by the deposition of fibrinogen might contribute to the development of the inflammatory response during ischemia reperfusion. The structural properties of fibrinogen play a key role in its interactions with various biomolecules and cell types.Fibrinogen is a 340-kDa plasma glycoprotein with a complex structure. The fibrinogen molecule consists of 2 identical subunits, each composed of 3 nonidentical polypeptide chains, A␣, B␤, and ␥. These chains are linked together by 29 disulfide bonds and form several structural regions, 2 distal D regions, one central E region, and 2 ␣C regions. 7 Each pair of distal nodules is linked with the central nodule by a triple helical coiled-coil connector composed of the middle po...

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“…The zero kinetic off‐rate ( k diss ) and the distance of the transition state ( x diss ) were estimated to be 3.78 × 10 −4 s −1 and 0.16 nm, respectively. For the fibrinogen–fibrin system, a dissociation rate of 3.6 × 10 −4 s −1 was estimated by extrapolating data from solution experiments involving a resonant mirror biosensor 49. The excellent agreement between this and the FS value suggests that the unbinding forces measured by the latter technique are determined by the same energy barrier that governs spontaneous dissociation in solution.…”

Section: Resultsmentioning

confidence: 94%

Force spectroscopy of the fibrin(ogen)–fibrinogen interaction

2007

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Fibrin aggregation is of vital importance in many physiological and pathological processes, such as blood coagulation, wound healing, and thrombosis. In the present study, we investigated the forces involved in the initial steps of the fibrinogen fibrin aggregation by force spectroscopy using the atomic force microscope. Our data confirm the existence of strong specific interactions between fibrin and fibrin(ogen), with unbinding forces ranging from 290 to 375 pN and a logarithmic dependence on the loading rate between 0.8 and 23 nN/s. © 2007 Wiley Periodicals, Inc. Biopolymers 89: 292–301, 2008. This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com

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Kinetics of the interaction of desAABB–fibrin monomer with immobilized fibrinogen

Cited by 11 publications

References 56 publications

Role of ‘B‐b’ knob‐hole interactions in fibrin binding to adsorbed fibrinogen

Role of ‘B‐b’ knob‐hole interactions in fibrin binding to adsorbed fibrinogen

Fibrinopeptides A and B release in the process of surface fibrin formation

Force spectroscopy of the fibrin(ogen)–fibrinogen interaction

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