dr inż. Izabela Piechocka

Zakład Biosystemów i Miękkiej Materii (ZBiMM)
Pracownia Modelowania w Biologii i Medycynie (PMBM)
stanowisko: specjalista
telefon: (+48) 22 826 12 81 wew.: 423
pokój: 328
e-mail: ipiech

Doktorat
2011-11-23 Biopolymers: from structural hierarchy to nonlinear rheology  (VUA)
promotor -- prof. dr G.H. Koenderink, AMOLF
promotor pomocniczy -- prof. dr F.C. MacKintosh, VU
1341 
Ostatnie publikacje
1.Piechocka I.K., Kurniawan N.A., Grimbergen J., Koopman J., Koenderink G.H., Recombinant fibrinogen reveals the differential roles of α- and γ-chain cross-linking and molecular heterogeneity in fibrin clot strain-stiffening, Journal of Thrombosis and Haemostasis, ISSN: 1538-7933, DOI: 10.1111/jth.13650, Vol.15, No.5, pp.938-949, 2017

Streszczenie:

Essentials Fibrinogen circulates in human plasma as a complex mixture of heterogeneous molecular variants. We measured strain-stiffening of recombinantly produced fibrinogen upon clotting. Factor XIII and molecular heterogeneity alter clot elasticity at the protofibril and fiber level. This highlights the hitherto unknown role of molecular composition in fibrin clot mechanics.

Słowa kluczowe:

blood coagulation, elasticity, fibrin, polymers, rheology, turbidimetry

Afiliacje autorów:

Piechocka I.K.-other affiliation
Kurniawan N.A.-Eindhoven University of Technology (NL)
Grimbergen J.-ProFibrix BV (NL)
Koopman J.-ProFibrix BV (NL)
Koenderink G.H.-FOM Institute AMOLF (NL)
40p.
2.Piechocka I.K., Jansen K.A., Broedersz C.P., Kurniawan N.A., MacKintosh F.C., Koenderink G.H., Multi-scale strain-stiffening of semiflexible bundle networks, SOFT MATTER, ISSN: 1744-683X, DOI: 10.1039/c5sm01992c, Vol.12, No.7, pp.2145-2156, 2016

Streszczenie:

Bundles of polymer filaments are responsible for the rich and unique mechanical behaviors of many biomaterials, including cells and extracellular matrices. In fibrin biopolymers, whose nonlinear elastic properties are crucial for normal blood clotting, protofibrils self-assemble and bundle to form networks of semiflexible fibers. Here we show that the extraordinary strain-stiffening response of fibrin networks is a direct reflection of the hierarchical architecture of the fibrin fibers. We measure the rheology of networks of unbundled protofibrils and find excellent agreement with an affine model of extensible wormlike polymers. By direct comparison with these data, we show that physiological fibrin networks composed of thick fibers can be modeled as networks of tight protofibril bundles. We demonstrate that the tightness of coupling between protofibrils in the fibers can be tuned by the degree of enzymatic intermolecular crosslinking by the coagulation factor XIII. Furthermore, at high stress, the protofibrils contribute independently to the network elasticity, which may reflect a decoupling of the tight bundle structure. The hierarchical architecture of fibrin fibers can thus account for the nonlinearity and enormous elastic resilience characteristic of blood clots.

Afiliacje autorów:

Piechocka I.K.-other affiliation
Jansen K.A.-FOM Institute AMOLF (NL)
Broedersz C.P.-Princeton University (US)
Kurniawan N.A.-Eindhoven University of Technology (NL)
MacKintosh F.C.-Vrije Universiteit (NL)
Koenderink G.H.-FOM Institute AMOLF (NL)
40p.
3.Jansen K.A., Bacabac R.G., Piechocka I.K., Koenderink G.H., Cells actively stiffen fibrin networks by generating contractile stress, BIOPHYSICAL JOURNAL, ISSN: 0006-3495, DOI: 10.1016/j.bpj.2013.10.008, Vol.105, No.10, pp.2240-2251, 2013

Streszczenie:

During wound healing and angiogenesis, fibrin serves as a provisional extracellular matrix. We use a model system of fibroblasts embedded in fibrin gels to study how cell-mediated contraction may influence the macroscopic mechanical properties of their extracellular matrix during such processes. We demonstrate by macroscopic shear rheology that the cells increase the elastic modulus of the fibrin gels. Microscopy observations show that this stiffening sets in when the cells spread and apply traction forces on the fibrin fibers. We further show that the stiffening response mimics the effect of an external stress applied by mechanical shear. We propose that stiffening is a consequence of active myosin-driven cell contraction, which provokes a nonlinear elastic response of the fibrin matrix. Cell-induced stiffening is limited to a factor 3 even though fibrin gels can in principle stiffen much more before breaking. We discuss this observation in light of recent models of fibrin gel elasticity, and conclude that the fibroblasts pull out floppy modes, such as thermal bending undulations, from the fibrin network, but do not axially stretch the fibers. Our findings are relevant for understanding the role of matrix contraction by cells during wound healing and cancer development, and may provide design parameters for materials to guide morphogenesis in tissue engineering.

Afiliacje autorów:

Jansen K.A.-FOM Institute AMOLF (NL)
Bacabac R.G.-Institute for Atomic and Molecular Physics (NL)
Piechocka I.K.-other affiliation
Koenderink G.H.-FOM Institute AMOLF (NL)
35p.
4.Piechocka I.K., van Oosten A.S.G., Breuls R.G., Koenderink G.H., Rheology of Heterotypic Collagen Networks, BIOMACROMOLECULES, ISSN: 1525-7797, DOI: 10.1021/bm200553x, Vol.12, No.7, pp.2797-2805, 2011

Streszczenie:

Collagen fibrils are the main structural element of connective tissues. In many tissues, these fibrils contain two fibrillar collagens (types I and V) in a ratio that changes during tissue development, regeneration, and various diseases. Here we investigate the influence of collagen composition on the structure and rheology of networks of purified collagen I and V, combining fluorescence and atomic force microscopy, turbidimetry, and rheometry. We demonstrate that the network stiffness strongly decreases with increasing collagen V content, even though the network structure does not substantially change. We compare the rheological data with theoretical models for rigid polymers and find that the elasticity is dominated by nonaffine deformations. There is no analytical theory describing this regime, hampering a quantitative interpretation of the influence of collagen V. Our findings are relevant for understanding molecular origins of tissue biomechanics and for guiding rational design of collagenous biomaterials for biomedical applications.

Afiliacje autorów:

Piechocka I.K.-other affiliation
van Oosten A.S.G.-University of Pennsylvania (US)
Breuls R.G.-Vrije Universiteit (NL)
Koenderink G.H.-FOM Institute AMOLF (NL)
40p.
5.Piechocka I.K., Bacabac R.G., Potters M., MacKintosh F.C., Koenderink G.H., Structural Hierarchy Governs Fibrin Gel Mechanics, BIOPHYSICAL JOURNAL, ISSN: 0006-3495, DOI: 10.1016/j.bpj.2010.01.040, Vol.98, No.10, pp.2281-2289, 2010

Streszczenie:

Fibrin gels are responsible for the mechanical strength of blood clots, which are among the most resilient protein materials in nature. Here we investigate the physical origin of this mechanical behavior by performing rheology measurements on reconstituted fibrin gels. We find that increasing levels of shear strain induce a succession of distinct elastic responses that reflect stretching processes on different length scales. We present a theoretical model that explains these observations in terms of the unique hierarchical architecture of the fibers. The fibers are bundles of semiflexible protofibrils that are loosely connected by flexible linker chains. This architecture makes the fibers 100-fold more flexible to bending than anticipated based on their large diameter. Moreover, in contrast with other biopolymers, fibrin fibers intrinsically stiffen when stretched. The resulting hierarchy of elastic regimes explains the incredible resilience of fibrin clots against large deformations.

Afiliacje autorów:

Piechocka I.K.-other affiliation
Bacabac R.G.-Institute for Atomic and Molecular Physics (NL)
Potters M.-Vrije Universiteit (NL)
MacKintosh F.C.-Vrije Universiteit (NL)
Koenderink G.H.-FOM Institute AMOLF (NL)
32p.

Abstrakty konferencyjne
1.Pawłowska S., Nakielski P., Pierini F., Zembrzycki K., Piechocka I.K., Kowalewski T.A., Tumbling, rotating and coiling of nanofilaments in an oscillating microchannel flow, BioNano6, Biomolecules and Nanostructures 6, 2017-05-10/05-14, Podlesice (PL), No.41E, pp.60, 2017
2.Nakielski P., Pierini F., Piechocka I.K., Blood clotting in the contact with nanofibers, NanoTech, NanoTech Poland International Conference & Exhibition, 2017-06-01/06-03, Poznań (PL), pp.178-178, 2017

Streszczenie:

Nanofibers have received considerable attention in the past years, mainly due to their vast application in medicine [1]. One of the fastest growing areas of application are wound dressings and hemostats. Among the major causes of death from trauma, massive bleeding is responsible for 30 – 40% of mortality. In the hospital, massive bleeding are the second most common cause of death (22%) just after cardiac factors (33%) [2].
Despite a large number of experiments done in the topic of blood-biomaterial interactions, coagulation mechanisms are still not fully understood. Therefore, the main objective of our work is the analysis of protein adsorption, platelet adhesion and aggregation, and blood plasma coagulation in the contact with polymer nanofibers. Various synthetic polymers, their blends with natural polymers of confirmed hemostatic effect e.g. collagen and gelatine, and additionally nanofibers made of chitosan are investigated for their potential to stop bleeding. In the final, controlled release of drugs affecting coagulation cascade will be an important step providing accelerated blood clot formation.

Afiliacje autorów:

Nakielski P.-IPPT PAN
Pierini F.-IPPT PAN
Piechocka I.K.-IPPT PAN