Grafting of methyl methacrylate and its derivatives onto blood

Kojima, Kuniharu; Iwabuchi, Susumu; Kojima, Kensuke; Tarumi, N; Masuhara, E

doi:10.1002/pol.1971.150091111

Cited by 11 publications

(2 citation statements)

References 8 publications

(4 reference statements)

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“…There have been many reports of tri-n-butylborane-initiated graft copolymerization of MMA onto proteins [8][9][10][11][12][13]; for example, the grafting of methyl methacrylate (MMA) onto collagen [8], chitin [9], cotton [10], silk fiber [11], blood [12], and hemoglobin [13]. These applications have been investigated over the course of the last four decades.…”

Section: Hohmentioning

confidence: 99%

Tri-n-Butylborane/WaterComplex-Mediated Copolymerization of Methyl Methacrylate with Proteinaceous Materials and Proteins: A Review

Fujisawa

Kadoma

2010

Polymers

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Previous studies of tri-n-butylborane-initiated graft copolymerization of methyl methacrylates with hydrated proteinous materials and proteins have focused on the number of grafted-poly (MMA) branches as well as the percent graft and graft efficiency. The number of branches in silk fibroin is 1.3, whereas the number in collagen, gelatin, ovalbumin and wool are 0.1, 0.04, 0.02 and 0.03, respectively. The number of grafted-PMMA branches in synthetic poly-L-peptides is approximately 10-fold less than that in gelatin, and decline, in the order poly-Ala > poly-Ser > poly-Pro > poly-Glu > poly-Lys. By contrast, poly-Gly, poly-Tyr and poly-Leu have no branches. The co-catalytic effect (the ratio of the number of polymer formed relative to that of control) of amino acids on tri-n-butylborane-initiated polymerization of MMA in the presence of water has been linearly correlated with their ionization potential (IP koopman ); |Äå HOMO (Highest Occupied Molecular Orbital)| (r 2 = 0.6, outliers: Cys and His); Äå HOMO = [åHOMO aqua − åHOMO vacuum ] calculated using the semiempirical AM1 method. Also, a significant exponential relationship between the number of branches of poly-L-polypeptides and the Äå HOMO of the corresponding amino acids has been observed (r 2 = 0.9). A possible grafting site of protein (polypeptide) is discussed.

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Section: Hohmentioning

confidence: 99%

Tri-n-Butylborane/WaterComplex-Mediated Copolymerization of Methyl Methacrylate with Proteinaceous Materials and Proteins: A Review

Fujisawa

Kadoma

2010

Polymers

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“…Recently, Kojima et a1. 16 have indicated that the basic amino acids, such as histidine and lysine, may play an important role in the grafting of methyl methacrylate by tri-n -butylborane onto blood proteins. In the present case, the contents of these basic amino acids in the grafted SCMKA remained unchanged.…”

Section: Keratin-polyacrylonitrile Copolymer 789mentioning

confidence: 99%

Membranes prepared from keratin–polyacrylonitrile graft copolymers

Schaller

Miyamoto

Shimamura

et al. 1980

J of Applied Polymer Sci

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SynopsisGraft copolymerization of acrylonitrile onto a soluble wool keratin derivative was studied with the reduced and carboxymethylated low-sulfur protein fraction from wool. Copolymerization was carried out under a variety of conditions with a redox system of ( N H~)~S~O B -N~~S O~ in 60% (w/w) aqueous ZnCl2 solution at 10°C. Monomer conversions higher than 90% were obtained by the stepwise addition of initiator. The graft products were successfully separated into grafted copolymer and homopolyacrylonitrile (PAN) by fractional precipitation or solvent extraction with DMF. Grafted PAN were isolated by acid hydrolysis of the keratin backbone. Characterization of grafted and homo-PAN was carried out by IR spectroscopy, amino acid endgroup analysis, and viscometry. On the basis of the results, effects of polymerization conditions on grafting parameters were discussed. Membranes were prepared from 60% aqueous ZnCl2 solution by using ice-cold water as the regenerating medium. All the membranes formed from the graft products were transparent. Observation by scanning electron microscopy showed that the surface consisted of rather spherical keratin domains regularly distributed in the PAN matrix. Selective hydrolysis of the keratin domains allowed a new type of porous PAN membrane to be obtained, with the inner walls of the pores being charged with amino acid residues attached to PAN chains as the endgroup.

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The grafting of methyl methacrylate onto cotton by tri‐n‐butylborane

Kojima

Iwabuchi

Murakami

et al. 1972

J of Applied Polymer Sci

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SynopsisMethyl methacrylate was grafted onto cotton by tri-n-butylborane in the presence of water. No graft was obtained in organic solvents, i.e., in the absence of water. The percentage of grafting increased with increases in reaction time, cotton amount, and initiator concentration. Pretreatment of cotton with pyridine also enhanced the percentage of grafting. Glycidyl methacrylate and ethyl acrylate were grafted onto cotton by tri-n-butylborane, while no grafting occurred when vinyl acetate and 4-vinyl pyridine were used. Usual radical initiators, such as azobisisobutyronitrile and benzoyl peroxide/ dimethyl-p-toluidine, were not effective under the same conditions.

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Grafting of methyl methacrylate and its derivatives onto blood

Cited by 11 publications

References 8 publications

Tri-n-Butylborane/WaterComplex-Mediated Copolymerization of Methyl Methacrylate with Proteinaceous Materials and Proteins: A Review

Tri-n-Butylborane/WaterComplex-Mediated Copolymerization of Methyl Methacrylate with Proteinaceous Materials and Proteins: A Review

Membranes prepared from keratin–polyacrylonitrile graft copolymers

The grafting of methyl methacrylate onto cotton by tri‐n‐butylborane

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