Physical bioenergetics of degradation-resistant proteins in diseases and aging

Axelsson, S.

doi:10.1016/s0306-9877(98)90253-5

Cited by 5 publications

(3 citation statements)

References 17 publications

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“…[7][8][9] These stereochemically modified proteins exhibit higher thermal stability and resistance to protease activity. [8][9][10] The rate of conversion from one configuration to another is an intrinsic property of each amino acid. Typically, for aspartic acid (Asp), alanine (Ala), glutamic acid (Glu), leucine (Leu), and isoleucine (Ile), the rate varies respectively as Asp > Ala ) Glu > Leu ) Ile.…”

Section: Introductionmentioning

confidence: 99%

“…In nature, biological compounds are stereospecific. For example, the amino acids (AA) in proteins are exclusively found as l stereoisomers. , Due to aging, the l → d configurational change has been observed in proteins such as collagen. − The exposure to UV radiation and high-temperature conditions can also induce l → d conversion in proteins. − These stereochemically modified proteins exhibit higher thermal stability and resistance to protease activity. − The rate of conversion from one configuration to another is an intrinsic property of each amino acid. Typically, for aspartic acid (Asp), alanine (Ala), glutamic acid (Glu), leucine (Leu), and isoleucine (Ile), the rate varies respectively as Asp > Ala = Glu > Leu = Ile …”

Section: Introductionmentioning

confidence: 99%

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Molecular Dynamics Investigations on the Effect of d Amino Acid Substitution in a Triple-Helix Structure and the Stability of Collagen

et al. 2009

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Studies on the structure and stability of peptides and proteins during l-->d configurational change are certainly important for the designing of peptides with new biological activity and protein engineering. The l-->d amino acid (d AA) changes have been observed in aged proteins such as collagen. Hence, in this study, an attempt has been made to explore the effect of the replacement of l amino acid (l AA) in the model collagen-like peptides with d AA and the origin of structural stability (destability) has been traced using the molecular dynamics (MD) method employing the AMBER force field. Our results reveal that the substitution of d AA produces a large local disruption to the triple-helical structure. Formation of a kink (bulge) at the site of substitution is observed from the detailed analysis of MD trajectory. However, this local perturbation of kinked helix changes the direction of the helices and affects the relative orientation of the respective AA residues for helix-helix interaction, enough to affect the overall stability of the model collagen-like peptide. The destabilization energy per d Ala substitution is 7.87 kcal/mol, which is similar to the value for the Gly-->Ala mutation in collagen. Since the Gly-->Ala mutation is involved in genetic disorders such as osteogenesis imperfecta (OI), the l-->d configurational change may produce a similar effect on collagen.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Molecular Dynamics Investigations on the Effect of d Amino Acid Substitution in a Triple-Helix Structure and the Stability of Collagen

et al. 2009

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“…Furthermore, connections have been suggested between BSE and Creutzfeldt-Jakob Disease and its variant (CJD, nCJD) (Chechler and Vincent, 2002). A primary change in handedness (particle spin, chirality) in some amino acids in peptides or whole post-translated proteins is one suggested possibility (Axelsson, 1998). However, this molecular configurations.…”

Section: Introductionmentioning

confidence: 99%

Cholinesterases and Unified Neurophysics

Axelsson

2007

Neuroquantology

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The enigmatic diseases of the 'Mad Cow' type (BSE) were approached from the fundamental level of ethereal particle spin (chirality). A revised definition of chirality then gave a logical explanation for structure and function in both physics and biology. Cholinesterases (ChEs) appeared to govern stereo-chemical hydrodynamics by the release of free protons to activate hem-transported molecular oxygen. Oxidation will increase stability of bio-molecules and recycle hydrogen to water. Biology stands for the only break in universal symmetry (parity violation) by its ChE-oxidative hydrodynamics and explains the matter-antimatter issue. In the brain, basic physical events will be inhibited, delayed or converted by ChE's hydrodynamic autonomy, which basically equals continuous inflammation. The pathophysiology in a lot of neurological diseases of the Bowine Spongioform Encephalitis -scrapie-Alzheimer's disease -Creutzfeldt-Jakob Disease type in cattle, sheep and man, like the relentless process of aging by long-term oxidative effects was elucidated by the present short glimpses into physics.

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Cholinergic regulation of biological hydrodynamics

Axelsson

2000

Medical Hypotheses

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Physical bioenergetics of degradation-resistant proteins in diseases and aging

Cited by 5 publications

References 17 publications

Molecular Dynamics Investigations on the Effect of d Amino Acid Substitution in a Triple-Helix Structure and the Stability of Collagen

Molecular Dynamics Investigations on the Effect of d Amino Acid Substitution in a Triple-Helix Structure and the Stability of Collagen

Cholinesterases and Unified Neurophysics

Cholinergic regulation of biological hydrodynamics

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