Surface FTIR Techniques to Analyze the Conformation of Proteins/ Peptides in H2O Environment

Combs, Joseph Dale; Gonzalez, Cuauhtemoc U; Wang, Chengshan

doi:10.4172/2161-0398.1000202

Cited by 5 publications

(4 citation statements)

References 50 publications

(111 reference statements)

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“… 33,41,42,45 Although they contribute significantly to the Amide‐II region, their bands show large homogeneity between MD1 and MD2, the two different medulla components, as well as the surrounding cortex, MF. As previously mentioned, this is most likely to be due to the Amide‐II region containing many overlapping contributions including plausible contributions from ring vibrational modes which could contribute differently to the constituent bands 37–39,47,48 . In the MF component, the parallel β‐sheet form (band 11) dominates (cf.…”

Section: Resultsmentioning

confidence: 95%

“…Localised AFM‐IR spectra from each of the structures can be further analysed in greater detail to characterise their specific chemistry, in an analogous fashion to that employed for bulk FTIR spectra, except that here it is on a nanometre scale. Qualitative comparisons show significant intensity differences at 1165, 1250 and 1300 cm −1 (Figure 3), assigned respectively to bands of cysteine oxidation products, the Amide‐III protein bands, and a combination between some higher‐frequency Amide‐III bands with C‐H and C‐C bands dominated by Tryptophan 28,32–39 . Nevertheless, although there are differences in the intensities of the MD1 and MF structures, their spectral profiles are notably similar, suggesting similar chemical structures.…”

Section: Resultsmentioning

confidence: 97%

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Using hybrid atomic force microscopy and infrared spectroscopy (AFM‐IR) to identify chemical components of the hair medulla on the nanoscale

Fellows

Casford

Davies

2021

Journal of Microscopy

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Atomic force microscopy integrated with infrared spectroscopy (AFM‐IR) has been used to topographically and chemically examine the medulla of human hair fibres with nanometre scale lateral resolution. The mapping of cross‐sections of the medulla showed two distinct structural components which were subsequently characterised spectroscopically. One of these components was shown to be closely similar to cortical cell species, consistent with the fibrillar structures found in previous electron microscope (EM) investigations. The other component showed large chemical differences from cortical cells and was assigned to globular vacuole species, also confirming EM observations. Further characterisation of the two components was achieved through spectral deconvolution of the protein Amide‐I and ‐II bands. This showed that the vacuoles have a greater proportion of the most thermodynamically stable conformation, namely the antiparallel β‐sheet structures. This chimes with the observed lower cysteine concentration, indicating a lower proportion of restrictive disulphide cross‐link bonding. Furthermore, the large α‐helix presence within the vacuoles points to a loss of matrix‐like material as well as significant intermolecular stabilisation of the protein structures. By analysing the carbonyl stretching region, it was established that the fibrillar, cortical cell‐like components showed considerable stabilisation from H‐bonding interactions, similar to the cortex, involving amino acid side chains whereas, in contrast, the vacuoles were found to only be stabilised significantly by structural lipids.

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Section: Resultsmentioning

confidence: 95%

Section: Resultsmentioning

confidence: 97%

Using hybrid atomic force microscopy and infrared spectroscopy (AFM‐IR) to identify chemical components of the hair medulla on the nanoscale

Fellows

Casford

Davies

2021

Journal of Microscopy

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“…Both SF-I and SF-II MCs show a strong peak at 1725 cm -1, indicating the presence of PLGA (shell) on the surfaces as can be expected [20]. Similarly, a peak belonging to bending vibration for the amine group (NH 2 ) from 1550 to 1650 cm -1 can be seen in SPI, SF-I, and SF-II spectra [21]. Spectra for PVA, SPI, SF-I, and SF-II MCs demonstrate an absorption peak at around 2900 cm -1 for the valence C-H vibration [22].…”

Section: Atr-ftir Analysismentioning

confidence: 57%

Elongated soy protein isolate-poly(D, L-lactide-co-glycolic acid) microcapsules prepared using syringe filters and their effect on self-healing efficiency of soy protein-based green resin

Shi

Netravali

2022

J Polym Environ

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A self-healing soy-based resin lled with soy protein isolate (SPI) containing poly(D, L-lactide-co-glycolic acid) (PLGA) microcapsules (MCs) was prepared. MCs were prepared using a syringe lter via a membrane emulsi cation technique. Using this method, spherical (diameter of about 1.30 μm) and elongated MCs (aspect ratios up to 20) could be produced. Tensile properties and self-healing e ciencies of resins were characterized for both MC morphologies in terms of strength recovery and toughness recovery. While both MCs could successfully heal cracks, spherical MCs were seen to compromise the tensile properties of the resin, whereas elongated MCs demonstrated some mechanical enhancement. Overall results showed that elongated MCs having a higher aspect ratio resulted in slightly better selfhealing performance as well as a mechanical improvement. The results also show that higher MC loading results in higher self-healing e ciency.

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“…The amide I band (mainly from the stretching mode of C=O in the amide group), www.nature.com/scientificreports/ amide II bands (from the bending mode vibration of N-H in amide group), and amide III (CN stretching, NH bending) are in the range of 1600-1700 cm −1 , 1500-1560 cm −1 , and below 1400 cm −1 , respectively 14 . Among all the amide bands, the position of the amide I band is most sensitive to the conformation (i.e., the secondary structures) change of proteins/peptides and has been widely used to evaluate the fraction of various secondary structures in a protein/peptide 30 . The result of this study showed α-helical structure of native buforin I (maxima in the Amide I band 1655 cm −1 ) was not affected by adding His-taq to the C-terminal of its amino acid sequence.…”

Section: Discussionmentioning

confidence: 99%

Effects of adding poly-histidine tag on stability, antimicrobial activity and safety of recombinant buforin I expressed in periplasmic space of Escherichia coli

Roshanak

Yarabbi

Shahidi

et al. 2023

Sci Rep

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The lack of cost-effective methods for producing antimicrobial peptides has made it impossible to use their high potential as a new and powerful class of antimicrobial agents. In recent years, extensive research has been conducted to decrease the cost of recombinant proteins production through microorganisms, transgenic animals, and plants. Well-known genetic and physiological characteristics, short-term proliferation, and ease of manipulation make E. coli expression system a valuable host for recombinant proteins production. Expression in periplasmic space is recommended to reduce the inherently destructive behavior of antimicrobial peptides against the expressing microorganism and to decline susceptibility to proteolytic degradation. In this study, a pET-based expression system was used to express buforin I at E. coli periplasmic space, and its antimicrobial, hemolytic, and cell toxicity activities as well as structural stability were evaluated. The hemolysis activity and cytotoxicity of His-tagged buforin I were negligible and its antimicrobial activity did not show a significant difference compared to synthetic buforin I. In addition, in silico investigating of stability of native and His-tagged buforin I showed that RMSF, RMSD and Rg curves had followed a similar trend during 150 ns simulation. Furthermore, evaluating the modelled structures, FTIR and X-ray methods of both peptides indicated an insignificant structural difference. It was concluded that the recombinant buforin I could be a viable alternative to some currently used antibiotics by successfully expressing it in the pET-based expression system.

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Surface FTIR Techniques to Analyze the Conformation of Proteins/ Peptides in H2O Environment

Cited by 5 publications

References 50 publications

Using hybrid atomic force microscopy and infrared spectroscopy (AFM‐IR) to identify chemical components of the hair medulla on the nanoscale

Using hybrid atomic force microscopy and infrared spectroscopy (AFM‐IR) to identify chemical components of the hair medulla on the nanoscale

Elongated soy protein isolate-poly(D, L-lactide-co-glycolic acid) microcapsules prepared using syringe filters and their effect on self-healing efficiency of soy protein-based green resin

Effects of adding poly-histidine tag on stability, antimicrobial activity and safety of recombinant buforin I expressed in periplasmic space of Escherichia coli

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