Carbonyl Contribution to the Excitation of Visible Fluorescence and Phosphorescence in Fibrous Proteins*

Kallman, Hartmut; Krasnansky, V. J.; Person, Philip

doi:10.1111/j.1751-1097.1968.tb05845.x

Cited by 8 publications

(7 citation statements)

References 10 publications

(1 reference statement)

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“…Our observations with multiple amino acids, several polyamino acids and different proteins from various suppliers extend earlier findings with individual proteins [16, 18], protein crystals [9, 32], polypeptide spherulites [8] and amyloid fibrils [6, 7]. When including not just inter- and intramolecular hydrogen bonding but allowing for hydrogen-bonding with water, our observations are for the most part consistent with previously suggested models of dbAF.…”

Section: Discussionsupporting

confidence: 90%

“…The earliest mention is by Kallman et al who recorded dbAF emission from collagen. [ 18 ] More recently, Guptasarma collected similar dbAF spectra from both γ-B crystallin and lysozyme. [ 16 ] Both agree well with our observations.…”

Section: Resultsmentioning

confidence: 99%

“…Following our identification of carbonyls, we found one reference 50 years back implicating carbonyls as source of collagen fluorescence, but without proof of its origin at the single amino acid level or any detailed physiochemical characterization. [ 18 ] This earlier observation was apparently discredited as artifact of UV-induced photoproducts of collagen that can be phosphorescent. [ 28 ] As we point out above, the wide variety of proteins, polypeptides and single amino acids exhibiting this fluorescence, and its close association with both carbonyl double bonds and its congruence with aggregation-induced fluorescence suggest that this earlier observation was likely correct.…”

Section: Resultsmentioning

confidence: 99%

“…The original findings by Kallman et al of dbAF in collagen were believed to be contaminated by photochemically induced fluorescent byproducts of collagen. [ 18 ] It is worth noting that this investigation into potential dbAF from proteins was prompted only by prior reports of significant dbAF from amyloid fibrils. [ 6 ] Lifetimes in the nanosecond range established that fibrillar dbAF, measured from amyloid fibrils, resulted from a resonant fluorescence emission instead of some inelastic scattering process.…”

Section: Discussionmentioning

confidence: 99%

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Carbonyl-based blue autofluorescence of proteins and amino acids

Niyangoda

Miti

Breydo³

et al. 2017

PLoS ONE

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Intrinsic protein fluorescence is inextricably linked to the near-UV autofluorescence of aromatic amino acids. Here we show that a novel deep-blue autofluorescence (dbAF), previously thought to emerge as a result of protein aggregation, is present at the level of monomeric proteins and even poly- and single amino acids. Just as its aggregation-related counterpart, this autofluorescence does not depend on aromatic residues, can be excited at the long wavelength edge of the UV and emits in the deep blue. Differences in dbAF excitation and emission peaks and intensities from proteins and single amino acids upon changes in solution conditions suggest dbAF’s sensitivity to both the chemical identity and solution environment of amino acids. Autofluorescence comparable to dbAF is emitted by carbonyl-containing organic solvents, but not those lacking the carbonyl group. This implicates the carbonyl double bonds as the likely source for the autofluorescence in all these compounds. Using beta-lactoglobulin and proline, we have measured the molar extinction coefficients and quantum yields for dbAF in the monomeric state. To establish its potential utility in monitoring protein biophysics, we show that dbAF emission undergoes a red-shift comparable in magnitude to tryptophan upon thermal denaturation of lysozyme, and that it is sensitive to quenching by acrylamide. Carbonyl dbAF therefore provides a previously neglected intrinsic optical probe for investigating the structure and dynamics of amino acids, proteins and, by extension, DNA and RNA.

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Section: Discussionsupporting

confidence: 90%

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

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Carbonyl-based blue autofluorescence of proteins and amino acids

Niyangoda

Miti

Breydo³

et al. 2017

PLoS ONE

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“…Cells were stained with DAPI and Phalloidin‐iFluor(TM) 594 conjugate. ELR‐fibers were visualized by taking advantage of their intrinsic autofluorescence (which has been associated with the carbonyl groups). g–h) ELR fibers lacking RGD motifs after cell seeding and i) cells seeded on BSA‐coated coverslip.…”

mentioning

confidence: 99%

Combining Catalyst‐Free Click Chemistry with Coaxial Electrospinning to Obtain Long‐Term, Water‐Stable, Bioactive Elastin‐Like Fibers for Tissue Engineering Applications

Fernández‐Colino

Wolf

Rütten

et al. 2018

Macromolecular Bioscience

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Elastic fibers are a fundamental requirement for tissue-engineered equivalents of physiologically elastic native tissues. Here, a simple one-step electrospinning approach is developed, combining i) catalyst-free click chemistry, ii) coaxial electrospinning, and iii) recombinant elastin-like polymers as a relevant class of biomaterials. Water-stable elastin-like fibers are obtained without the use of cross-linking agents, catalysts, or harmful organic solvents. The fibers can be directly exposed to an aqueous environment at physiological temperature and their morphology maintained for at least 3 months. The bioactivity of the fibers is demonstrated with human vascular cells and the potential of the process for vascular tissue engineering is shown by fabricating small-diameter tubular fibrous scaffolds. Moreover, highly porous fluffy 3D constructs are obtained without the use of specially designed collectors or sacrificial materials, further supporting their applicability in the biomedical field. Ultimately, the strategy that is developed here may be applied to other click systems, contributing to expanding their potential in medical technology.

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Luminescence of Polypeptides and Proteins

Longworth

1971

Excited States of Proteins and Nucleic Acids

155

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Carbonyl Contribution to the Excitation of Visible Fluorescence and Phosphorescence in Fibrous Proteins*

Cited by 8 publications

References 10 publications

Carbonyl-based blue autofluorescence of proteins and amino acids

Carbonyl-based blue autofluorescence of proteins and amino acids

Combining Catalyst‐Free Click Chemistry with Coaxial Electrospinning to Obtain Long‐Term, Water‐Stable, Bioactive Elastin‐Like Fibers for Tissue Engineering Applications

Luminescence of Polypeptides and Proteins

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