Probing the Folding Mechanism of a Leucine Zipper Peptide by Stopped-Flow Circular Dichroism Spectroscopy

Zitzewitz, Jill A.; Bilsel, Osman; Luo, Jiabin; Jones, Bryan E.; Matthews, C. Robert

doi:10.1021/bi00039a042

Cited by 200 publications

(219 citation statements)

References 45 publications

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“…A variety of studies have already been conducted on the thermodynamics and kinetics of unfolding equilibria for the GCN4 coiled-coil. Most results are in agreement that the GCN4 coiled-coil monomer-dimer transition follows a two-state equilibrium [36][37][38][39], although there is some evidence that there is more than one folded form [40,41]. Circular dichroic spectroscopy studies were conducted to assess the folding of the PF4 ZIP under various conditions.…”

Section: Oligomerization Of Pf4 Zipmentioning

confidence: 82%

Manipulation of hydrogel assembly and growth factor delivery via the use of peptide–polysaccharide interactions

Zhang

Furst

Kiick

2006

Journal of Controlled Release

116

131

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The design of materials in which assembly, mechanical response, and biological properties are controlled by protein-polysaccharide interactions could provide materials that mimic the biological environment and find use in the delivery of growth factors. In the investigations reported here, a heparin-binding, coiled-coil peptide, PF4 ZIP , was employed to mediate the assembly of heparinized polymers. The heparin-binding affinity of this peptide was compared with that of other heparinbinding peptides (HBP) via heparin-sepharose chromatography and surface plasmon resonance (SPR) experiments. Results from these experiments indicate that PF4 ZIP demonstrates a higher heparin-binding affinity and heparin association rate when compared to the heparin-binding domains of antithrombin III (ATIII) and heparin-interacting protein (HIP). Viscoelastic hydrogels were formed upon the association of PF4 ZIP -functionalized star poly(ethylene glycol) (PEG-PF4 ZIP ) with low-molecular-weight heparin-functionalized star PEG (PEG-LMWH). The viscoelastic properties of the hydrogels can be altered via variations in the ratio of LMWH to PF4 ZIP . bFGF release from these gels have also been investigated. Comparison of the bFGF release profiles with the hydrogel erosion profiles indicates that bFGF delivery from this class of hydrogels is mainly an erosioncontrolled process and the rates of bFGF release can be modulated via choice of HBP or via variations in the mechanical properties of the hydrogels. Manipulation of hydrogel physical properties and erosion profiles will provide novel materials for controlled growth factor delivery and other biomedical applications.

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Section: Oligomerization Of Pf4 Zipmentioning

confidence: 82%

Manipulation of hydrogel assembly and growth factor delivery via the use of peptide–polysaccharide interactions

Zhang

Furst

Kiick

2006

Journal of Controlled Release

116

131

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“…Thermodynamic stabilities of other fourhelix bundles (Munson et al, 1994;Bryson et al, 1995) and coiled coils (Harbury et al, 1993;Lumb et al, 1994;Zitzewitz et al, 1995) formed from similar length peptides or similar numbers of amino acid residues, are similar to free energies of association/ folding for /?pep-4. For examples, AG values are -8.1 kcal/mol, -7.3 kcal/mol, and -7.5 kcal/mol, respectively, for folding dimeric four-helix bundles Ropll, Ropl3, and Rop21 (Munson et al, 1994); -7.8 kcal/mol for folding alpha 3, another dimeric four-helix bundle (Kaumaya et al, 1990), and -10.5 kcal/mol for folding the leucine zipper peptide 33mer GCN4-pl (Zitzewitz et al, 1995). Notice that most of these free energies are for formation of dimers and are very close to the /?pep4 AGD value of -7.3 kcal/mol.…”

Section: Discussionmentioning

confidence: 99%

A folding pathway for βpep‐4 peptide 33mer: From unfolded monomers and β‐sheet sandwich dimers to well‐structured tetramers

Mayo

Ilyina

1998

Protein Science

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It was recently reported that a de novo designed peptide 33mer, Ppep-4, can form well-structured P-sheet sandwich tetramers (Ilyina E, Roongta V, Mayo KH, 1997b, Biochemistry 36:5245-5250). For insight into the pathway of Ppep-4 folding, the present study investigates the concentration dependence of Ppep-4 self-association by using 'H-NMR pulsedfield gradient (PFG)-NMR diffusion measurements, and circular dichroism. Downfield chemically shifted a H resonances, found to arise only from the well-structured Ppep-4 tetramer state, yield the fraction of tetramer within the oligomer equilibrium distribution. PFG-NMR-derived diffusion coefficients, D, provide a means for deriving the contribution of monomer and other oligomer states to this distribution. These data indicate that tetramer is the highest oligomer state formed, and that inclusion of monomer and dimer states in the oligomer distribution is sufficient to explain the concentration dependence of D values for /.?pep-4. Equilibrium constants calculated from these distributions [2.5 X lo5 M" for M-D and 1.2 X lo4 M-' for D-T at 31 3 K] decrease only slightly, if at all, with decreasing temperature indicating a hydrophobically mediated, entropy-driven association/folding process. Conformational analyses using NMR and CD provide a picture where "random coil" monomers associate to form molten globule-like P-sheet sandwich dimers that further associate and fold as well-structured tetramers. /.?pep-4 folding is thermodynamically linked to self-association. As with folding of singlechain polypeptides, the final folding step to well-structured tetramer ppep-4 is rate limiting.

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“…These results are compared with those reported recently for smaller coiled coils (Mo et al, 1991a,b;Wendt et al, 1995;Zitzewitz et al, 1995) and their biological relevance is discussed.…”

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confidence: 55%

Kinetics of Folding of the Myosin Rod

Béchet

Nozais

1997

European Journal of Biochemistry

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The kinetics of the unfolding and refolding of the myosin rod have been studied by fluorescence and circular dichroism techniques, at different concentrations of protein and guanidine hydrochloride. The unfolding of the myosin rod was fast and at least biphasic in 2-3 M denaturant, with an initial immediate phase followed by a slower low-amplitude first-order phase. The refolding of the rod in 0.4-2 M guanidine hydrochloride was also at least biphasic; an initial immediate phase preceded a slow second-order phase. At the final denaturant concentration of 0.8 M, the amplitude of the burst phase was weakly dependent on the protein concentration and the rate constant of the refolding slow phase was optimal. These data are incorporated into a folding mechanism with at least three states. The high rates of the first steps of unfolding and refolding may be relevant for the functioning of the native myosin molecule by allowing a transient separation of the two strands of the myosin tail.

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Probing the Folding Mechanism of a Leucine Zipper Peptide by Stopped-Flow Circular Dichroism Spectroscopy

Cited by 200 publications

References 45 publications

Manipulation of hydrogel assembly and growth factor delivery via the use of peptide–polysaccharide interactions

Manipulation of hydrogel assembly and growth factor delivery via the use of peptide–polysaccharide interactions

A folding pathway for βpep‐4 peptide 33mer: From unfolded monomers and β‐sheet sandwich dimers to well‐structured tetramers

Kinetics of Folding of the Myosin Rod

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