Preferential photochemical interaction of Ru (III) doped carbon nano dots with bovine serum albumin over human serum albumin
The excitation wavelength dependent emission of carbon nano dots (CNDs) restricts their use in photophysical studies. However, instead of bare CNDs, the amine coated Ru (III) doped CNDs (Ru:CNDEDAs) are quite eligible to generate excitation wavelength independent fluorescence with high quantum yield...
Ausführliche Beschreibung
Autor*in: |
Maity, Arnab [verfasserIn] Pal, Uttam [verfasserIn] Chakraborty, Brotati [verfasserIn] Sengupta, Chaitrali [verfasserIn] Sau, Abhishek [verfasserIn] Chakraborty, Swatadipta [verfasserIn] Basu, Samita [verfasserIn] |
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Format: |
E-Artikel |
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Sprache: |
Englisch |
Erschienen: |
2019 |
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Schlagwörter: |
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Übergeordnetes Werk: |
Enthalten in: International journal of biological macromolecules - New York, NY [u.a.] : Elsevier, 1979, 137, Seite 483-494 |
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Übergeordnetes Werk: |
volume:137 ; pages:483-494 |
DOI / URN: |
10.1016/j.ijbiomac.2019.06.126 |
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Katalog-ID: |
ELV002740230 |
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520 | |a The excitation wavelength dependent emission of carbon nano dots (CNDs) restricts their use in photophysical studies. However, instead of bare CNDs, the amine coated Ru (III) doped CNDs (Ru:CNDEDAs) are quite eligible to generate excitation wavelength independent fluorescence with high quantum yield. Herein, we report a detailed study on the photochemical interaction between two different serum albumins, bovine serum albumin (BSA) and human serum albumin (HSA), with Ru:CNDEDAs synthesized in our laboratory, using steady-state and time-resolved spectroscopic techniques. Absorption study reveals the formation of ground state complex between Ru:CNDEDAs and BSA/HSA while the circular dichroism study implies that Ru:CNDEDAs perturbs the secondary structure of the albumin proteins. Steady-state fluorescence study helps in understanding energy transfer from tryptophan, the fluorophore moiety of BSA and HSA, to Ru:CNDEDAs. Time-resolved studies within nanosecond time domain clarify the phenomenon of energy transfer from BSA/HSA to Ru:CNDEDAs with varied efficiency. Molecular dynamic simulation ascertains that the efficiency of energy transfer is highly dependent on the stability of protein-nanoparticle complex. This study provides a qualitative description regarding the structural rigidity of transport protein, BSA compared to HSA, which determines the transport ability of CNDs to deliver the desired drug molecule to the targeted cells. | ||
650 | 4 | |a Carbon nano dots | |
650 | 4 | |a Serum albumin | |
650 | 4 | |a Fluorescence | |
700 | 1 | |a Pal, Uttam |e verfasserin |4 aut | |
700 | 1 | |a Chakraborty, Brotati |e verfasserin |4 aut | |
700 | 1 | |a Sengupta, Chaitrali |e verfasserin |4 aut | |
700 | 1 | |a Sau, Abhishek |e verfasserin |4 aut | |
700 | 1 | |a Chakraborty, Swatadipta |e verfasserin |4 aut | |
700 | 1 | |a Basu, Samita |e verfasserin |4 aut | |
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10.1016/j.ijbiomac.2019.06.126 doi (DE-627)ELV002740230 (ELSEVIER)S0141-8130(19)33091-0 DE-627 ger DE-627 rda eng 540 570 DE-600 BIODIV DE-30 fid 35.80 bkl 58.30 bkl Maity, Arnab verfasserin aut Preferential photochemical interaction of Ru (III) doped carbon nano dots with bovine serum albumin over human serum albumin 2019 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier The excitation wavelength dependent emission of carbon nano dots (CNDs) restricts their use in photophysical studies. However, instead of bare CNDs, the amine coated Ru (III) doped CNDs (Ru:CNDEDAs) are quite eligible to generate excitation wavelength independent fluorescence with high quantum yield. Herein, we report a detailed study on the photochemical interaction between two different serum albumins, bovine serum albumin (BSA) and human serum albumin (HSA), with Ru:CNDEDAs synthesized in our laboratory, using steady-state and time-resolved spectroscopic techniques. Absorption study reveals the formation of ground state complex between Ru:CNDEDAs and BSA/HSA while the circular dichroism study implies that Ru:CNDEDAs perturbs the secondary structure of the albumin proteins. Steady-state fluorescence study helps in understanding energy transfer from tryptophan, the fluorophore moiety of BSA and HSA, to Ru:CNDEDAs. Time-resolved studies within nanosecond time domain clarify the phenomenon of energy transfer from BSA/HSA to Ru:CNDEDAs with varied efficiency. Molecular dynamic simulation ascertains that the efficiency of energy transfer is highly dependent on the stability of protein-nanoparticle complex. This study provides a qualitative description regarding the structural rigidity of transport protein, BSA compared to HSA, which determines the transport ability of CNDs to deliver the desired drug molecule to the targeted cells. Carbon nano dots Serum albumin Fluorescence Pal, Uttam verfasserin aut Chakraborty, Brotati verfasserin aut Sengupta, Chaitrali verfasserin aut Sau, Abhishek verfasserin aut Chakraborty, Swatadipta verfasserin aut Basu, Samita verfasserin aut Enthalten in International journal of biological macromolecules New York, NY [u.a.] : Elsevier, 1979 137, Seite 483-494 Online-Ressource (DE-627)30089502X (DE-600)1483284-7 (DE-576)259270814 1879-0003 nnns volume:137 pages:483-494 GBV_USEFLAG_U SYSFLAG_U GBV_ELV FID-BIODIV SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_224 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2336 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4313 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4393 35.80 Makromolekulare Chemie 58.30 Biotechnologie AR 137 483-494 |
spelling |
10.1016/j.ijbiomac.2019.06.126 doi (DE-627)ELV002740230 (ELSEVIER)S0141-8130(19)33091-0 DE-627 ger DE-627 rda eng 540 570 DE-600 BIODIV DE-30 fid 35.80 bkl 58.30 bkl Maity, Arnab verfasserin aut Preferential photochemical interaction of Ru (III) doped carbon nano dots with bovine serum albumin over human serum albumin 2019 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier The excitation wavelength dependent emission of carbon nano dots (CNDs) restricts their use in photophysical studies. However, instead of bare CNDs, the amine coated Ru (III) doped CNDs (Ru:CNDEDAs) are quite eligible to generate excitation wavelength independent fluorescence with high quantum yield. Herein, we report a detailed study on the photochemical interaction between two different serum albumins, bovine serum albumin (BSA) and human serum albumin (HSA), with Ru:CNDEDAs synthesized in our laboratory, using steady-state and time-resolved spectroscopic techniques. Absorption study reveals the formation of ground state complex between Ru:CNDEDAs and BSA/HSA while the circular dichroism study implies that Ru:CNDEDAs perturbs the secondary structure of the albumin proteins. Steady-state fluorescence study helps in understanding energy transfer from tryptophan, the fluorophore moiety of BSA and HSA, to Ru:CNDEDAs. Time-resolved studies within nanosecond time domain clarify the phenomenon of energy transfer from BSA/HSA to Ru:CNDEDAs with varied efficiency. Molecular dynamic simulation ascertains that the efficiency of energy transfer is highly dependent on the stability of protein-nanoparticle complex. This study provides a qualitative description regarding the structural rigidity of transport protein, BSA compared to HSA, which determines the transport ability of CNDs to deliver the desired drug molecule to the targeted cells. Carbon nano dots Serum albumin Fluorescence Pal, Uttam verfasserin aut Chakraborty, Brotati verfasserin aut Sengupta, Chaitrali verfasserin aut Sau, Abhishek verfasserin aut Chakraborty, Swatadipta verfasserin aut Basu, Samita verfasserin aut Enthalten in International journal of biological macromolecules New York, NY [u.a.] : Elsevier, 1979 137, Seite 483-494 Online-Ressource (DE-627)30089502X (DE-600)1483284-7 (DE-576)259270814 1879-0003 nnns volume:137 pages:483-494 GBV_USEFLAG_U SYSFLAG_U GBV_ELV FID-BIODIV SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_224 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2336 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4313 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4393 35.80 Makromolekulare Chemie 58.30 Biotechnologie AR 137 483-494 |
allfields_unstemmed |
10.1016/j.ijbiomac.2019.06.126 doi (DE-627)ELV002740230 (ELSEVIER)S0141-8130(19)33091-0 DE-627 ger DE-627 rda eng 540 570 DE-600 BIODIV DE-30 fid 35.80 bkl 58.30 bkl Maity, Arnab verfasserin aut Preferential photochemical interaction of Ru (III) doped carbon nano dots with bovine serum albumin over human serum albumin 2019 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier The excitation wavelength dependent emission of carbon nano dots (CNDs) restricts their use in photophysical studies. However, instead of bare CNDs, the amine coated Ru (III) doped CNDs (Ru:CNDEDAs) are quite eligible to generate excitation wavelength independent fluorescence with high quantum yield. Herein, we report a detailed study on the photochemical interaction between two different serum albumins, bovine serum albumin (BSA) and human serum albumin (HSA), with Ru:CNDEDAs synthesized in our laboratory, using steady-state and time-resolved spectroscopic techniques. Absorption study reveals the formation of ground state complex between Ru:CNDEDAs and BSA/HSA while the circular dichroism study implies that Ru:CNDEDAs perturbs the secondary structure of the albumin proteins. Steady-state fluorescence study helps in understanding energy transfer from tryptophan, the fluorophore moiety of BSA and HSA, to Ru:CNDEDAs. Time-resolved studies within nanosecond time domain clarify the phenomenon of energy transfer from BSA/HSA to Ru:CNDEDAs with varied efficiency. Molecular dynamic simulation ascertains that the efficiency of energy transfer is highly dependent on the stability of protein-nanoparticle complex. This study provides a qualitative description regarding the structural rigidity of transport protein, BSA compared to HSA, which determines the transport ability of CNDs to deliver the desired drug molecule to the targeted cells. Carbon nano dots Serum albumin Fluorescence Pal, Uttam verfasserin aut Chakraborty, Brotati verfasserin aut Sengupta, Chaitrali verfasserin aut Sau, Abhishek verfasserin aut Chakraborty, Swatadipta verfasserin aut Basu, Samita verfasserin aut Enthalten in International journal of biological macromolecules New York, NY [u.a.] : Elsevier, 1979 137, Seite 483-494 Online-Ressource (DE-627)30089502X (DE-600)1483284-7 (DE-576)259270814 1879-0003 nnns volume:137 pages:483-494 GBV_USEFLAG_U SYSFLAG_U GBV_ELV FID-BIODIV SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_224 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2336 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4313 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4393 35.80 Makromolekulare Chemie 58.30 Biotechnologie AR 137 483-494 |
allfieldsGer |
10.1016/j.ijbiomac.2019.06.126 doi (DE-627)ELV002740230 (ELSEVIER)S0141-8130(19)33091-0 DE-627 ger DE-627 rda eng 540 570 DE-600 BIODIV DE-30 fid 35.80 bkl 58.30 bkl Maity, Arnab verfasserin aut Preferential photochemical interaction of Ru (III) doped carbon nano dots with bovine serum albumin over human serum albumin 2019 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier The excitation wavelength dependent emission of carbon nano dots (CNDs) restricts their use in photophysical studies. However, instead of bare CNDs, the amine coated Ru (III) doped CNDs (Ru:CNDEDAs) are quite eligible to generate excitation wavelength independent fluorescence with high quantum yield. Herein, we report a detailed study on the photochemical interaction between two different serum albumins, bovine serum albumin (BSA) and human serum albumin (HSA), with Ru:CNDEDAs synthesized in our laboratory, using steady-state and time-resolved spectroscopic techniques. Absorption study reveals the formation of ground state complex between Ru:CNDEDAs and BSA/HSA while the circular dichroism study implies that Ru:CNDEDAs perturbs the secondary structure of the albumin proteins. Steady-state fluorescence study helps in understanding energy transfer from tryptophan, the fluorophore moiety of BSA and HSA, to Ru:CNDEDAs. Time-resolved studies within nanosecond time domain clarify the phenomenon of energy transfer from BSA/HSA to Ru:CNDEDAs with varied efficiency. Molecular dynamic simulation ascertains that the efficiency of energy transfer is highly dependent on the stability of protein-nanoparticle complex. This study provides a qualitative description regarding the structural rigidity of transport protein, BSA compared to HSA, which determines the transport ability of CNDs to deliver the desired drug molecule to the targeted cells. Carbon nano dots Serum albumin Fluorescence Pal, Uttam verfasserin aut Chakraborty, Brotati verfasserin aut Sengupta, Chaitrali verfasserin aut Sau, Abhishek verfasserin aut Chakraborty, Swatadipta verfasserin aut Basu, Samita verfasserin aut Enthalten in International journal of biological macromolecules New York, NY [u.a.] : Elsevier, 1979 137, Seite 483-494 Online-Ressource (DE-627)30089502X (DE-600)1483284-7 (DE-576)259270814 1879-0003 nnns volume:137 pages:483-494 GBV_USEFLAG_U SYSFLAG_U GBV_ELV FID-BIODIV SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_224 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2336 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4313 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4393 35.80 Makromolekulare Chemie 58.30 Biotechnologie AR 137 483-494 |
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10.1016/j.ijbiomac.2019.06.126 doi (DE-627)ELV002740230 (ELSEVIER)S0141-8130(19)33091-0 DE-627 ger DE-627 rda eng 540 570 DE-600 BIODIV DE-30 fid 35.80 bkl 58.30 bkl Maity, Arnab verfasserin aut Preferential photochemical interaction of Ru (III) doped carbon nano dots with bovine serum albumin over human serum albumin 2019 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier The excitation wavelength dependent emission of carbon nano dots (CNDs) restricts their use in photophysical studies. However, instead of bare CNDs, the amine coated Ru (III) doped CNDs (Ru:CNDEDAs) are quite eligible to generate excitation wavelength independent fluorescence with high quantum yield. Herein, we report a detailed study on the photochemical interaction between two different serum albumins, bovine serum albumin (BSA) and human serum albumin (HSA), with Ru:CNDEDAs synthesized in our laboratory, using steady-state and time-resolved spectroscopic techniques. Absorption study reveals the formation of ground state complex between Ru:CNDEDAs and BSA/HSA while the circular dichroism study implies that Ru:CNDEDAs perturbs the secondary structure of the albumin proteins. Steady-state fluorescence study helps in understanding energy transfer from tryptophan, the fluorophore moiety of BSA and HSA, to Ru:CNDEDAs. Time-resolved studies within nanosecond time domain clarify the phenomenon of energy transfer from BSA/HSA to Ru:CNDEDAs with varied efficiency. Molecular dynamic simulation ascertains that the efficiency of energy transfer is highly dependent on the stability of protein-nanoparticle complex. This study provides a qualitative description regarding the structural rigidity of transport protein, BSA compared to HSA, which determines the transport ability of CNDs to deliver the desired drug molecule to the targeted cells. Carbon nano dots Serum albumin Fluorescence Pal, Uttam verfasserin aut Chakraborty, Brotati verfasserin aut Sengupta, Chaitrali verfasserin aut Sau, Abhishek verfasserin aut Chakraborty, Swatadipta verfasserin aut Basu, Samita verfasserin aut Enthalten in International journal of biological macromolecules New York, NY [u.a.] : Elsevier, 1979 137, Seite 483-494 Online-Ressource (DE-627)30089502X (DE-600)1483284-7 (DE-576)259270814 1879-0003 nnns volume:137 pages:483-494 GBV_USEFLAG_U SYSFLAG_U GBV_ELV FID-BIODIV SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_224 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2336 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4313 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4393 35.80 Makromolekulare Chemie 58.30 Biotechnologie AR 137 483-494 |
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540 570 DE-600 BIODIV DE-30 fid 35.80 bkl 58.30 bkl Preferential photochemical interaction of Ru (III) doped carbon nano dots with bovine serum albumin over human serum albumin Carbon nano dots Serum albumin Fluorescence |
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Preferential photochemical interaction of Ru (III) doped carbon nano dots with bovine serum albumin over human serum albumin |
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Preferential photochemical interaction of Ru (III) doped carbon nano dots with bovine serum albumin over human serum albumin |
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Maity, Arnab Pal, Uttam Chakraborty, Brotati Sengupta, Chaitrali Sau, Abhishek Chakraborty, Swatadipta Basu, Samita |
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preferential photochemical interaction of ru (iii) doped carbon nano dots with bovine serum albumin over human serum albumin |
title_auth |
Preferential photochemical interaction of Ru (III) doped carbon nano dots with bovine serum albumin over human serum albumin |
abstract |
The excitation wavelength dependent emission of carbon nano dots (CNDs) restricts their use in photophysical studies. However, instead of bare CNDs, the amine coated Ru (III) doped CNDs (Ru:CNDEDAs) are quite eligible to generate excitation wavelength independent fluorescence with high quantum yield. Herein, we report a detailed study on the photochemical interaction between two different serum albumins, bovine serum albumin (BSA) and human serum albumin (HSA), with Ru:CNDEDAs synthesized in our laboratory, using steady-state and time-resolved spectroscopic techniques. Absorption study reveals the formation of ground state complex between Ru:CNDEDAs and BSA/HSA while the circular dichroism study implies that Ru:CNDEDAs perturbs the secondary structure of the albumin proteins. Steady-state fluorescence study helps in understanding energy transfer from tryptophan, the fluorophore moiety of BSA and HSA, to Ru:CNDEDAs. Time-resolved studies within nanosecond time domain clarify the phenomenon of energy transfer from BSA/HSA to Ru:CNDEDAs with varied efficiency. Molecular dynamic simulation ascertains that the efficiency of energy transfer is highly dependent on the stability of protein-nanoparticle complex. This study provides a qualitative description regarding the structural rigidity of transport protein, BSA compared to HSA, which determines the transport ability of CNDs to deliver the desired drug molecule to the targeted cells. |
abstractGer |
The excitation wavelength dependent emission of carbon nano dots (CNDs) restricts their use in photophysical studies. However, instead of bare CNDs, the amine coated Ru (III) doped CNDs (Ru:CNDEDAs) are quite eligible to generate excitation wavelength independent fluorescence with high quantum yield. Herein, we report a detailed study on the photochemical interaction between two different serum albumins, bovine serum albumin (BSA) and human serum albumin (HSA), with Ru:CNDEDAs synthesized in our laboratory, using steady-state and time-resolved spectroscopic techniques. Absorption study reveals the formation of ground state complex between Ru:CNDEDAs and BSA/HSA while the circular dichroism study implies that Ru:CNDEDAs perturbs the secondary structure of the albumin proteins. Steady-state fluorescence study helps in understanding energy transfer from tryptophan, the fluorophore moiety of BSA and HSA, to Ru:CNDEDAs. Time-resolved studies within nanosecond time domain clarify the phenomenon of energy transfer from BSA/HSA to Ru:CNDEDAs with varied efficiency. Molecular dynamic simulation ascertains that the efficiency of energy transfer is highly dependent on the stability of protein-nanoparticle complex. This study provides a qualitative description regarding the structural rigidity of transport protein, BSA compared to HSA, which determines the transport ability of CNDs to deliver the desired drug molecule to the targeted cells. |
abstract_unstemmed |
The excitation wavelength dependent emission of carbon nano dots (CNDs) restricts their use in photophysical studies. However, instead of bare CNDs, the amine coated Ru (III) doped CNDs (Ru:CNDEDAs) are quite eligible to generate excitation wavelength independent fluorescence with high quantum yield. Herein, we report a detailed study on the photochemical interaction between two different serum albumins, bovine serum albumin (BSA) and human serum albumin (HSA), with Ru:CNDEDAs synthesized in our laboratory, using steady-state and time-resolved spectroscopic techniques. Absorption study reveals the formation of ground state complex between Ru:CNDEDAs and BSA/HSA while the circular dichroism study implies that Ru:CNDEDAs perturbs the secondary structure of the albumin proteins. Steady-state fluorescence study helps in understanding energy transfer from tryptophan, the fluorophore moiety of BSA and HSA, to Ru:CNDEDAs. Time-resolved studies within nanosecond time domain clarify the phenomenon of energy transfer from BSA/HSA to Ru:CNDEDAs with varied efficiency. Molecular dynamic simulation ascertains that the efficiency of energy transfer is highly dependent on the stability of protein-nanoparticle complex. This study provides a qualitative description regarding the structural rigidity of transport protein, BSA compared to HSA, which determines the transport ability of CNDs to deliver the desired drug molecule to the targeted cells. |
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