Trehalose induced structural modulation of Bovine Serum Albumin at ambient temperature

Das, Ahana; Basak, Pijush; Pattanayak, Rudradip; Kar, Turban; Majumder, Rajib; Pal, Debadrita; Bhattacharya, A.; Bhattacharyya, Maitree; Banik, Samudra Prosad

doi:10.1016/j.ijbiomac.2017.07.074

Cited by 26 publications

(20 citation statements)

References 55 publications

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“…Many researchers have investigated the protective properties of different sugars on polypeptides, proteins and biomolecules [42][43][44]. It has been advocated that protein aggregation and denaturation can be prevented by using carbohydrates as protectants.…”

Section: Raman Spectroscopymentioning

confidence: 99%

3D printed microneedle patches using stereolithography (SLA) for intradermal insulin delivery

Economidou

Pere

Reid

et al. 2019

Materials Science and Engineering: C

208

113

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3D printed microneedle arrays were fabricated using a biocompatible resin through stereolithography (SLA) for transdermal insulin delivery. Microneedles were built by polymerising consecutive layers of a photopolymer resin. Thin layers of insulin and sugar alcohol or disaccharide carriers were formed on the needle surface by inkjet printing. The optimization of the printing process resulted in superior skin penetration capacity of the 3D printed microneedles compared to metal arrays with minimum applied forces varying within the range of 2 to 5N. Micro-CT analysis showed strong adhesion of the coated films on the microneedle surface even after penetration to the skin. In vivo animal trials revealed fast insulin action with excellent hypoglycaemia control and lower glucose levels achieved within 60 min, combined with steady state plasma glucose over 4 h compared to subcutaneous injections.

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Section: Raman Spectroscopymentioning

confidence: 99%

3D printed microneedle patches using stereolithography (SLA) for intradermal insulin delivery

Economidou

Pere

Reid

et al. 2019

Materials Science and Engineering: C

208

113

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“…However, it has been reported recently that sucrose compresses the tertiary structure but has no effect on the secondary structure of the ribosomal protein S6 23 . It has also been shown that trehalose compresses bovine serum albumin and increases its α-helicity 24 . But the mechanism of the structure change has not been addressed.…”

mentioning

confidence: 99%

Polyol and sugar osmolytes can shorten protein hydrogen bonds to modulate function

Chen

et al. 2020

Commun Biol

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Polyol and sugar osmolytes are commonly used in therapeutic protein formulations. How they may affect protein structure and function is an important question. In this work, through NMR measurements, we show that glycerol and sorbitol (polyols), as well as glucose (sugar), can shorten protein backbone hydrogen bonds. The hydrogen bond shortening is also captured by molecular dynamics simulations, which suggest a hydrogen bond competition mechanism. Specifically, osmolytes weaken hydrogen bonds between the protein and solvent to strengthen those within the protein. Although the hydrogen bond change is small, with the average experimental cross hydrogen bond 3hJNC′ coupling of two proteins GB3 and TTHA increased by ~ 0.01 Hz by the three osmolytes (160 g/L), its effect on protein function should not be overlooked. This is exemplified by the PDZ3−peptide binding where several intermolecular hydrogen bonds are formed and osmolytes shift the equilibrium towards the bound state.

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“…Trp-134 is fully solvent accessible being localized in the second helix of the first domain whereas Trp-212 is localized in a hydrophobic pocket of domain II. Therefore, BSA is an ideal model for probing structural transition due to polarity changes [ 30 , 68 , 69 ]. Especially, Trp-134 fluorescence is widely used to gain preliminary idea about the helix integrity of the protein [ 70 ].…”

Section: Resultsmentioning

confidence: 99%

“…The emission spectra were recorded between 315 to 500 nm. Baseline corrections were performed with buffer in all cases [ 30 , 31 ].…”

Section: Materials and Methodologymentioning

confidence: 99%

Ribosylation induced structural changes in Bovine Serum Albumin: understanding high dietary sugar induced protein aggregation and amyloid formation

Das

Basak

Pramanik

et al. 2020

Heliyon

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Non-enzymatic glycation of proteins is believed to be the root cause of high dietary sugar associated pathophysiological maladies. We investigated the structural changes in protein during progression of glycation using ribosylated Bovine Serum Albumin (BSA). Non enzymatic attachment of about 45 ribose molecules to BSA resulted in gradual reduction of hydrophobicity and aggregation as indicated by red-shifted tryptophan fluorescence, reduced ANS binding and lower anisotropy of FITC-conjugated protein. Parallely, there was a significant decrease of alpha helicity as revealed by Circular Dichroism (CD) and Fourier transformed-Infra Red (FT-IR) spectra. The glycated proteins assumed compact globular structures with enhanced Thioflavin-T binding resembling amyloids. The gross structural transition affected by ribosylation led to enhanced thermostability as indicated by melting temperature and Transmission Electron Microscopy. At a later stage of glycation, the glycated proteins developed non-specific aggregates with increase in size and loss of amyloidogenic behaviour. A parallel non-glycated control incubated under similar conditions indicated that amyloid formation and associated changes were specific for ribosylation and not driven by thermal denaturation due to incubation at 37 °C. Functionality of the glycated protein was significantly altered as probed by Isothermal Titration Calorimetry using polyphenols as substrates. The studies demonstrated that glycation driven globular amyloids form and persist as transient intermediates during formation of misfolded glycated adducts. To the best of our knowledge, the present study is the first systematic attempt to understand glycation associated changes in a protein and provides important insights towards designing therapeutics for arresting dietary sugar induced amyloid formation.

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Trehalose induced structural modulation of Bovine Serum Albumin at ambient temperature

Cited by 26 publications

References 55 publications

3D printed microneedle patches using stereolithography (SLA) for intradermal insulin delivery

3D printed microneedle patches using stereolithography (SLA) for intradermal insulin delivery

Polyol and sugar osmolytes can shorten protein hydrogen bonds to modulate function

Ribosylation induced structural changes in Bovine Serum Albumin: understanding high dietary sugar induced protein aggregation and amyloid formation

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