Dynamic force measurements of avidin-biotin and streptavidin-biotin interactions using AFM

• Autorzy: De O.-P. M. , Czuba P. , Targosz M. , Burda K. , Szymonski M.
• Języki publikacji: EN

Abstrakty

EN

Using atomic force microscopy (AFM) we performed dynamic force measurements of the adhesive forces in two model systems: avidin-biotin and streptavidin-biotin. In our experiments we used glutaraldehyde for immobilization of (strept)avidin on the tip and biotin on the sample surface. Such interface layers are more rigid than those usually reported in the literature for AFM studies, when (strept)avidin is coupled with biotinylated bovine albumin and biotin with agarose polymers. We determined the dependence of the rupture forces of avidin-biotin and streptavidin-biotin bonds in the range 300-9600 pN/s. The slope of a semilogarithmic plot of this relation changes at about 1700 pN/s. The existence of two different regimes indicates the presence of two activation barriers of these complexes during the dissociation process. The dissociation rates and activation energy barriers, calculated from the Bell model, for the avidin-biotin and streptavidin-biotin interactions are similar to each other for loading rates > 1700 pN/s but they are different from each other for loading rates < 1700 pN/s. In the latter case, the dissociation rates show a higher stability of the avidin-biotin complex than the streptavidin-biotin complex due to a larger outer activation barrier of 0.8 kBT. The bond-rupture force is about 20 pN higher for the avidin-biotin pair than for the streptavidin-biotin pair for loading rates < 1700 pN/s. These two experimental observations are in agreement with the known structural differences between the biotin binding pocket of avidin and of streptavidin.

Słowa kluczowe

EN

living process; atomic force microscopy; streptavidin-biotin model system; streptavidin; interaction; loading rate; dissociation rate; avidin-biotin model system; avidin; living organism; biotin

• Wydawca: -
• Czasopismo: Acta Biochimica Polonica
• Rocznik: 2006
• Tom: 53
• Numer: 1
• Opis fizyczny: p.93-100,fig.,ref.

Twórcy

autor

De O.-P. M.

• Polish Academy of Sciences, Krakow, Poland

autor

Czuba P.

autor

Targosz M.

autor

Burda K.

autor

Szymonski M.

Bibliografia

• Allen S, Davies J, Dawkes AC, Davies MC, Edwards JC, Parker MC, Roberts CJ, Sefton J, Tendler SJB, Williams PM (1996) In situ observation of streptavidin–biotin binding on an immunoassay well surface using an atomic force microscope. FEBS Lett 390: 161–164.
• Ashkin A, Dziedzic JM (1987) Optical trapping and manipulation of viruses and bacteria. Science 235: 1517–1520.
• Bayer EA, Wilchek M (1990) Application of avidin ± biotin technology to affinity-based separations. J Chromatog 510: 3–11.
• Bell GI (1978) Models for the specific adhesion of cells to cells. Science 200: 618–627.
• Binnig G, Quate CF, Gerber CH (1986) Atomic force microscopy. Phys Rev Lett 56: 930–933.
• Bongrand P (1999) Ligand–receptor interactions. Rep Prog Phys 62: 921–968.
• Dammer U, Hegner M, Anselmetti D, Wagner P, Dreier M, Huber W, Güntherodt HJ (1996) Specific antigen/antibody interactions measured by force microscopy. Biophys J 70: 2437–2441.
• Evans E, Ritchie K, Merkel R (1995) Sensitive force technique to probe molecular adhesion and structural linkages at biological interfaces. Biophys J 68: 2580–2587.
• Evans E, Ritchie K (1997) Dynamic strength of molecular adhesion bonds. Biophys J 72: 1541–1555.
• Fersht A (1985) Enzyme Structure and Mechanism. 2nd edn, WH Freeman and Company, New York.
• Florin E–L, Moy VT, Gaub HE (1994) Adhesion forces between individual ligand–receptor pairs. Science 264: 415–417.
• Freitag S, Le Trong I, Klumb L, Stayton PS, Stenkamp RE (1997) Structural studies of the streptavidin binding loop. Protein Sci 6: 1157–1166.
• Fritz JA, Katopodis G, Kolbinger F, Anselmetti D (1998) Force mediated kinetics of single P-selectin/ligand complexes observed by atomic force microscopy. Proc Natl Acad Sci USA 95: 12283–12288.
• Green NM (1975) Avidin. Adv Protein Chem 29: 85–133.
• Grubmüller H, Heymann B, Tavan P (1996) Ligand binding: molecular mechanics calculation of the streptavidin–biotin rupture force. Science 271: 997–999.
• Guttenberg Z, Bausch AR, Bin Hu, Bruinsma R, Morader L, Sackman E (2000) Measuring ligand–receptor unbinding forces with magnetic beads: molecular average. Langmuir 16: 8984–8993.
• Izrailev S, Stepaniants S, Balsera M, Oono Y, Schulten K (1997) Molecular dynamics study of unbinding of the avidin–biotin complex. Biophys J 72: 1568–1581.
• Kramers HA (1940) Brownian motion in a field of force and the diffusion model of chemical reactions. Physica 7: 284–302.
• Li Y, Li H, Yang F, Smith-Gill SJ, Mariuzza RA (2003) Xray snapshots of the maturation of an antibody response to a protein antigen. Nat Struct Biol 6: 482–488.
• Linvah O, Bayer EA, Wilchek M, Sussman JL (1993) Threedimential structure of avidin and the avidin–biotin complex. Proc Natl Acad Sci USA 90: 5076–5080.
• Lo YS, Zhu Y, Beebe TP (2001) Loading-rate dependence of individual ligand–receptor bond-rupture forces studied by atomic force microscopy. Langmuir 17: 3741–3748.
• Luckham PF, Smith K (1998) Direct measurements of the recognition forces between protein and membrane receptors. Faraday Disc 111: 307–320.
• Marttila AT, Hytönen VP, Laitinen OH, Bayer EA, Wilchek M, Kuomaa MS (2003) Mutation of the Tyr33 residue of chicken avidin: functional and structural consequences. Biochim J 369: 249–254.
• Merkel R, Nassoy P, Leung A, Ritchie K, Evans E (1999) Energy landscapes of receptor–ligand bonds explored with dynamic force spectroscopy. Nature 397: 50–53.
• Oberhauser AF, Marszalek PE, Erickson HP, Fernandez JM (1998) The molecular elasticity of the extracellular matrix tenascin. Nature 393: 181–185.
• Rief M, Oesterhelt F, Heymann B, Gaub HE (1997) Single molecule force spectroscopy on polysaccharides by atomic force microscopy. Science 275: 1295–1297.
• Sader JE, Chon JWM, Mulvaney P (1999) Calibration of rectangular atomic force microscope cantilevers. Rev Sci Instrum 70: 3967–3969.
• Sakahara H, Saga T (1999) Avidin–biotin system for delivery of diagnostic agents. Adv Drug Deliv Rev 37: 89–101.
• Schetters H (1999) Avidin and streptavidin in clinical diagnostics. Biomol Eng 17: 73–78.
• Weber PC, Ohlendorf DH, Wendoloski JJ, Salemme FR (1989) Structural origins of high affinity biotin binding to streptavidin. Science 243: 85–88.
• Wilchek M, Bayer EA (1999) Foreword and introduction to the book (Strept)avidin–biotin system. Biomol Eng 16: 1–4.
• Wong J, Chilkoti A, Moy VT (1999) Direct force measurements of streptavidin–biotin interaction. Biomol Eng 16: 45–55.
• Yuan Ch, Chen A, Kolb P, Moy VT (2000) Energy landscape of streptavidin–biotin complexes measured by atomic force microscopy. Biochemistry 39: 10219–10223.
• Zhang X, Moy VT (2003) Cooperative adhesion of ligand receptor bonds. Biophys Chem 104: 271–278.