Cotton functionalized with peptides: characterization and synthetic methods

Orlandin, Andrea; Formaggio, Fernando; Toffoletti, Antonio; Peggion, Cristina

doi:10.1002/psc.2659

Cited by 14 publications

(9 citation statements)

References 53 publications

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“…Furthermore, the bands at 3480 cm −1 and 3435 cm −1 may represent nanocellulose systems with a higher density of hydroxyl groups [50,59] compared to previously-reported cotton filter paper or print cloth [50]. The spectrum shows the amide peaks assigned to the tripeptide conjugate at 1652–1650 cm −1 (strong, literature value 1650) and 1568 cm −1 (weak, literature value 1540) [62,63,64]. The 1732 cm −1 band is indicative of C=O stretching vibrations (esters, aldehydes, e.g.…”

Section: Resultsmentioning

confidence: 99%

Preparation, Characterization and Activity of a Peptide-Cellulosic Aerogel Protease Sensor from Cotton

Edwards

Fontenot

Prevost

et al. 2016

Sensors

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Nanocellulosic aerogels (NA) provide a lightweight biocompatible material with structural properties, like interconnected high porosity and specific surface area, suitable for biosensor design. We report here the preparation, characterization and activity of peptide-nanocellulose aerogels (PepNA) made from unprocessed cotton and designed with protease detection activity. Low-density cellulosic aerogels were prepared from greige cotton by employing calcium thiocyanate octahydrate/lithium chloride as a direct cellulose dissolving medium. Subsequent casting, coagulation, solvent exchange and supercritical carbon dioxide drying afforded homogeneous cellulose II aerogels of fibrous morphology. The cotton-based aerogel had a porosity of 99% largely dominated by mesopores (2–50 nm) and an internal surface of 163 m2·g−1. A fluorescent tripeptide-substrate (succinyl-alanine-proline-alanine-4-amino-7-methyl-coumarin) was tethered to NA by (1) esterification of cellulose C6 surface hydroxyl groups with glycidyl-fluorenylmethyloxycarbonyl (FMOC), (2) deprotection and (3) coupling of the immobilized glycine with the tripeptide. Characterization of the NA and PepNA included techniques, such as elemental analysis, mass spectral analysis, attenuated total reflectance infrared imaging, nitrogen adsorption, scanning electron microscopy and bioactivity studies. The degree of substitution of the peptide analog attached to the anhydroglucose units of PepNA was 0.015. The findings from mass spectral analysis and attenuated total reflectance infrared imaging indicated that the peptide substrate was immobilized on to the surface of the NA. Nitrogen adsorption revealed a high specific surface area and a highly porous system, which supports the open porous structure observed from scanning electron microscopy images. Bioactivity studies of PepNA revealed a detection sensitivity of 0.13 units/milliliter for human neutrophil elastase, a diagnostic biomarker for inflammatory diseases. The physical properties of the aerogel are suitable for interfacing with an intelligent protease sequestrant wound dressing.

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Section: Resultsmentioning

confidence: 99%

Preparation, Characterization and Activity of a Peptide-Cellulosic Aerogel Protease Sensor from Cotton

Edwards

Fontenot

Prevost

et al. 2016

Sensors

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“…5a. Figure 5b shows the amide peaks assigned to the tetrapeptide conjugate at 1652-1650 cm -1 (strong, literature value 1650) and 1568 cm -1 (weak, literature value 1540) (Bellamy 1975;Orlandin et al 2014;Roeges 1994b). The ATR-IR results support the ESI-MS findings that the tetrapeptide is anchored on the surface of the biosensor.…”

Section: Molecular Surface Analysismentioning

confidence: 97%

Human neutrophil elastase peptide sensors conjugated to cellulosic and nanocellulosic materials: part I, synthesis and characterization of fluorescent analogs

et al. 2016

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Here we describe the synthesis and characterization of peptide conjugated cellulose and nanocellulose materials as sensors for fluorescent detection of human neutrophil elastase (HNE). The cellulose sensor surfaces selected are filter paper (FP) and print cloth (PC) fabric, which are composed of processed cotton fibers. The nanocellulose based sensors have transducer surfaces comprised of cellulose nanocrystals (wCNC) and microfibrillated cellulose (MFC) derived from wood that are fabricated as wood nanocellulose composites (wNCCs) consisting of blended quantities of nanocrystalline and MFC at 66/33 and 50/50 ratios. These ratios were selected to examine the effect of significantly different CNC loadings had on surface area and peptide uptake. The fluorescent peptide HNE substrate, n-succinyl-Ala-Pro-Ala-4-amido-7-methylcoumarin (Pep) was attached to both cellulosic and nanocellulosic matrices and conjugated peptide analogs were confirmed by mass spectrometry (MS) and infrared (IR). The nanocellulose biosensors wCNCPep (3c) and wNCC-Pep (4c, 66/33 and 5c, 50/50) have higher levels of peptide incorporation than the cellulosic biosensors FP-Pep (1c) and PC-Pep (2c). The range of incorporation for the cellulosic sensors is 7-25 lg/mg and for the nanocellulose sensors 30-80 lg/mg. The degree of substitution of peptide was found to be in the order of approximate number of peptides per 200 anhydroglucose residues, 1 in PC-Pep (2c), 2 in FP-Pep (1c), 4 in wNCC-Pep (5c, 50/50), 6 in wNCC-Pep (4c, 66/33), and 12 in wCNC-Pep (3c). The specific surface areas of the sensors ranged from 0.016 to 261 m 2 g -1 and correlated with degree of substitution of peptide on the cellulosic and nanocellulosic surfaces. Of the cellulose and nanocellulose biosensors, the wCNC-Pep (3c) has the highest level of peptide incorporation and the highest specific surface area, which makes it the preferred sensor matrix for human neutrophil elastase.

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“…The peptide-cotton samples were prepared according to a protocol previously set up in our laboratory [22,30]. Briefly, for each sample, a piece of cotton fabric of about 2 cm 2 was accurately weighed, washed with methanol (MeOH), N,N-dimethylformamide (DMF), MeOH and finally air-dried.…”

Section: Cotton Functionalizationmentioning

confidence: 99%

“…However, esters are not very stable at acidic or basic pH or in the presence of hydrolytic enzymes. Therefore, also in this contribution we carried out the covalent attachment of peptides to cellulose through an ether bond [30,31], by exploiting and improving a previous literature report [32]. The free hydroxyl groups of cellulose are directly functionalized, avoiding any oxidation or reduction reaction.…”

Section: Introductionmentioning

confidence: 98%

“…We built the peptides directly onto the cotton surface. After derivatization of the cellulose hydroxyl groups, cotton was used as the substrate for the 'solid phase' synthesis of peptides (SPPS) [30,41,50]. According to the same procedure, we also built Lys-based dendrimers [51][52][53] of the same peptides as their mechanism of membrane disruption requires the formation of clusters.…”

Section: Introductionmentioning

confidence: 99%

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Covalent Graft of Lipopeptides and Peptide Dendrimers to Cellulose Fibers

et al. 2019

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Introduction: Bacterial proliferation in health environments may lead to the development of specific pathologies, but can be highly dangerous under particular conditions, such as during chemotherapy. To limit the spread of infections, it is helpful to use gauzes and clothing containing antibacterial agents. As cotton tissues are widespread in health care environments, in this contribution we report the preparation of cellulose fibers characterized by the covalent attachment of lipopeptides as possible antimicrobial agents. Aim: To covalently link peptides to cotton samples and characterize them. Peptides are expected to preserve the features of the fabrics even after repeated washing and use. Peptides are well tolerated by the human body and do not induce resistance in bacteria. Materials and Methods: A commercially available cotton tissue (specific weight of 150 g/m2, 30 Tex yarn fineness, fabric density of 270/230 threads/10 cm in the warp and weft) was washed with alkali and bleached and died. A piece of this tissue was accurately weighed, washed with methanol (MeOH) and N,N-dimethylformamide (DMF), and air-dried. Upon incubation with epibromohydrin, followed by treatment with Fmoc-NH-CH2CH2-NH2 and Fmoc removal, the peptides were synthesized by incorporating one amino acid at a time, beginning with the formation of an amide bond with the free NH2 of 1,2–diaminoethane. We also linked to the fibers a few peptide dendrimers, because the mechanism of action of these peptides often requires the formation of clusters. We prepared and characterized seven peptide-cotton samples. Results: The new peptide-cotton conjugates were characterized by means of FT-IR spectroscopy and X-ray Photoelectron Spectroscopy (XPS). This latter technique allows for discriminating among different amino acids and thus different peptide-cotton samples. Some samples maintain a pretty good whiteness degree even after peptide functionalization. Interestingly, these samples also display encouraging activities against a Gram positive strain. Conclusions: Potentially antimicrobial lipopeptides can be covalently linked to cotton fabrics, step-by-step. It is also possible to build on the cotton Lys-based dendrimers. XPS is a useful technique to discriminate among different types of nitrogen. Two samples displaying some antibacterial potency did also preserve their whiteness index.

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Cotton functionalized with peptides: characterization and synthetic methods

Cited by 14 publications

References 53 publications

Preparation, Characterization and Activity of a Peptide-Cellulosic Aerogel Protease Sensor from Cotton

Preparation, Characterization and Activity of a Peptide-Cellulosic Aerogel Protease Sensor from Cotton

Human neutrophil elastase peptide sensors conjugated to cellulosic and nanocellulosic materials: part I, synthesis and characterization of fluorescent analogs

Covalent Graft of Lipopeptides and Peptide Dendrimers to Cellulose Fibers

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