Internal dynamics and protein–matrix coupling in trehalose-coated proteins

Cordone, Lorenzo; Cottone, Grazia; Giuffrida, Sergio; Palazzo, Gerardo; Venturoli, Giovanni; Viappiani, Cristiano

doi:10.1016/j.bbapap.2005.03.004

Cited by 126 publications

(220 citation statements)

References 178 publications

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“…The recombination phases that temporally precede the D→A phase are occurring under the modulating influence of those dynamics that do not require large global volume changing fluctuations. The large amplitude dynamics of the D state are readily damped in rigid media (Cordone et al, 1998;Dantsker et al, 2002;Librizzi et al, 2002;Abbruzzetti et al, 2005;Cordone et al, 2005;Dantsker et al, 2005a;Dantsker et al, 2005b). In glassy matrices they become manifest near or at the glass transition temperature of the surrounding solvent Dantsker et al, 2005a;Dantsker et al, 2005b).…”

Section: State Dynamicsmentioning

confidence: 99%

“…versus ~ 2×10 −5 seconds). The implication is that the volume changing D state protein dynamics suffer a proportionately greater degree of slow down when the solvent is comprised of a strong extended hydrogen bonded network of the kind that is formed from concentrated sugar-water mixtures involving trehalose (Cottone et al, 2001;Cordone et al, 2005;Cottone et al, 2005). The strong extended hydrogen bonded network is expected to increase the energy penalty associated with the large degree of solvent reorganization needed to accommodate the volume changing dynamics of the protein.…”

Section: Temperature Dependence For the C→d Transitions Is Solvent Dementioning

confidence: 99%

“…The C state dynamics are thermally activated but with low activation energies (Dantsker et al, 2005b) that are consistent with slaving to the β fluctuations of the hydration shell. They occur even in glassy matrices (Cordone et al, 1998;Librizzi et al, 2002;Abbruzzetti et al, 2005;Cordone et al, 2005;Dantsker et al, 2005a;Dantsker et al, 2005b) as long as the matrix is not totally rigidified as in the case of extremely dry glasses where only the B→A recombination phase is observed for COMb even at ambient temperatures . The C state dynamics appear to be associated primarily with side chain fluctuations that serve to: i) facilitate diffusion of the dissociated ligand both out of the distal hemepocket into the Xe cavities and between the accessible cavities of the protein, ii) transiently open connections between intra-protein cavities and iii) slightly enhance the enthalpic barrier for recombination through partial relaxation of side chains to positions that hinder access of the dissociated ligand to the heme iron.…”

mentioning

confidence: 99%

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Ligand recombination and a hierarchy of solvent slaved dynamics: The origin of kinetic phases in hemeproteins

Samuni

Dantsker

Roche

et al. 2007

Gene

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Ligand recombination studies play a central role both for characterizing different hemeproteins and there conformational states but also for probing fundamental biophysical processes. Consequently, there is great importance to providing a foundation from which one can understand the physical processes that give rise to and modulate the large range of kinetic patterns associated with ligand recombination in myoglobins and hemoglobins. In this work, an overview of cryogenic and solution phase recombination phenomena for COMb is first reviewed and then a new paradigm is presented for analyzing the temperature and viscosity dependent features of kinetic traces in terms of multiple phases that reflect which tier(s) of solvent-slaved protein dynamics is(are) operative on the photoproduct population during the time course of the measurement. This approach allows for facile inclusion of both ligand diffusion among accessible cavities and conformational relaxation effects. The concepts are illustrated using kinetic traces and MEM populations derived from the CO recombination process for wild type and mutant myoglobins either in sol-gel matrices bathed in glycerol or in trehalose derived glassy matrices. Keywords myoglobin; carbonmonoxide; sol-gel; trehalose; geminate recombination; Xe cavities Ligand recombinationStudies utilizing ligand recombination subsequent to photodissociation continue to provide basic insight into the functional properties of the many varieties of hemoglobin and myoglobin like molecules that are found through out the animal and plant worlds. Such studies are significant for several reasons all of which stem from the sensitivity of the recombination process to global structure, site specific effects and dynamics. Ligand recombination data at ambient temperatures are often useful in establishing potential functions of a newly described hemeproteins as well as routinely being used in exploring structure-function correlations in well characterized molecules such as human hemoglobin and mammalian myoglobins. Ligand recombination in myoglobin in particular has provided biophysics with a process that has allowed for dramatic advances in understanding: i) protein dynamics, ii) the role of protein dynamics in modulating protein reactivity and iii) the interplay between the dynamical properties of the protein and the surrounding solvent. Despite the heavy focus on understanding Publisher's Disclaimer: This is a PDF file of an unedited manuscript that has been accepted for publication. As a service to our customers we are providing this early version of the manuscript. The manuscript will undergo copyediting, typesetting, and review of the resulting proof before it is published in its final citable form. Please note that during the production process errors may be discovered which could affect the content, and all legal disclaimers that apply to the journal pertain. NIH Public Access Author ManuscriptGene. Author manuscript; available in PMC 2008 August 15. Published in final edited form as:Gene. 200...

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Section: State Dynamicsmentioning

confidence: 99%

Section: Temperature Dependence For the C→d Transitions Is Solvent Dementioning

confidence: 99%

mentioning

confidence: 99%

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Ligand recombination and a hierarchy of solvent slaved dynamics: The origin of kinetic phases in hemeproteins

Samuni

Dantsker

Roche

et al. 2007

Gene

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“…Infrared spectroscopy experiments 21 show that there is a large number of direct hydrogen bonds formed between trehalose and lysozyme, which is suggestive of the water replacement hypothesis. However, there is also much experimental [8][9][10][11] and theoretical 12,13,15,16 data showing that the protein-sugar interactions are better described in terms of water entrapment hypotheses.…”

Section: Introductionmentioning

confidence: 99%

Self-assembly of trehalose molecules on a lysozyme surface: the broken glass hypothesis

Fedorov

Goodman

Nerukh

et al. 2011

Phys. Chem. Chem. Phys.

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“…In general, stabilizing excipients are added to the proteins before spray drying to prevent degradation during processing and storage, where immobilization of the labile materials in an amorphous glass is believed to be advantageous for maintaining the activity of the incorporated molecules [21][22][23][24]. Disaccharides are amongst the most used excipients, with trehalose being particularly successful [25,26]. However, polyvinylpyrrolidone (PVP) is sometimes added when formulating proteins as a dry powder to prevent re-crystallization of stabilizing sugars and the thereby induced inactivation of incorporated labile materials during storage [27][28][29].…”

Section: Introductionmentioning

confidence: 99%

Spray drying of an attenuated live Newcastle disease vaccine virus intended for respiratory mass vaccination of poultry

Corbanie

Remon

Reeth

et al. 2007

Vaccine

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A powder vaccine intended for aerosol vaccination of poultry was formulated by spray drying a live attenuated Newcastle disease virus with potential stabilizers (mannitol, trehalose, polyvinylpyrrollidone (PVP), bovine serum albumin (BSA)). Thermodynamic properties, water sorption, particle size distribution, nebulization properties, density and morphology of the powders were evaluated and the virus survival during spray drying and storage was determined by incubation in embryonated eggs and subsequent haemagglutination assay. All powders had a narrow size distribution with a median volume diameter of ±30 m (suitable for primary respiratory vaccination of chickens) and good aerosolization characteristics. Four amorphous, hygroscopic formulations were produced (trehalose, trehalose-PVP, trehalose-BSA, trehalose-PVP-BSA), where addition of BSA was beneficial for virus survival during production and storage at 6 and 25 • C. A crystalline, non-hygroscopic powder (mannitol) had a lower stabilizing capacity during production but maintained the remaining virus titre during storage. In conclusion, the study demonstrates that it is possible to produce a dry powder formulation of an attenuated live vaccine for mass vaccination of poultry in a one-step spray drying process.

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Internal dynamics and protein–matrix coupling in trehalose-coated proteins

Cited by 126 publications

References 178 publications

Ligand recombination and a hierarchy of solvent slaved dynamics: The origin of kinetic phases in hemeproteins

Ligand recombination and a hierarchy of solvent slaved dynamics: The origin of kinetic phases in hemeproteins

Self-assembly of trehalose molecules on a lysozyme surface: the broken glass hypothesis

Spray drying of an attenuated live Newcastle disease vaccine virus intended for respiratory mass vaccination of poultry

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