The discovery of berberine erythrocyte-hemoglobin self-assembly delivery system: a neglected carrier underlying its pharmacokinetics
Berberine (BBR) has extremely low concentration and high tissue distribution. However, current pharmacokinetic studies predominantly focus on its concentration in plasma, which could hardly make a comprehensive understanding of its pharmacokinetic process. This study made a pioneering endeavor to ex...
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| Veröffentlicht in: | Drug delivery 2022-12, Vol.29 (1), p.856-870 |
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| creator | Yu, Qiuxia Li, Minhua Chen, Hanbin Xu, Lieqiang Cheng, Juanjuan Lin, Guoshu Liu, Yuhong Su, Ziren Yang, Xiaobo Li, Yucui Chen, Jiannan Xie, Jianhui |
| description | Berberine (BBR) has extremely low concentration and high tissue distribution. However, current pharmacokinetic studies predominantly focus on its concentration in plasma, which could hardly make a comprehensive understanding of its pharmacokinetic process. This study made a pioneering endeavor to explore the erythrocyte-hemoglobin (Hb) self-assembly system of BBR by exploring the interaction of BBR with erythrocyte and the combination of BBR with Hb. Results showed that BBR had a low bioavailability (C
0
= 2.833 μg/mL via intravenous administration of 2.5 mg/kg BBR and C
max
= 0.260 μg/mL via oral administration of 400 mg/kg BBR). Besides, BBR achieved higher concentrations in erythrocytes than plasma, and the erythrocytes count and Hb content were significantly decreased after intravenous administration. Hemolysis rate indicated the BBR-erythrocyte system (with 2% erythrocytes) was relatively stable without hemolysis at the concentration of 1.00 mg/mL. And the maximum percentage of drug loading was 100% when the BBR-erythrocyte concentration was 0.185 μg/mL. Furthermore, incubation of BBR and erythrocytes resulted in internalization of the erythrocyte membrane and the formation of intracellular vacuoles. The thermodynamic parameters indicated that the binding process of bovine hemoglobin (BHB) and BBR was spontaneous. UV-vis absorption spectra, synchronous fluorescence, circular dichroism and Raman spectra collectively indicated that BBR showed strong binding affinity toward BHB and affected the molecular environment of residues like tryptophan and tyrosine in BHB, resulting in the conformational changes of its secondary and tertiary structure. Molecular docking indicated BBR interacted with Arg-141 residue of BHB via hydrogen bond with the bond length of 2.55 Å. The ΔG value of the BHB-BBR system was −31.79 kJ/mol. Molecular dynamics simulation indicated the root mean square derivation of BBR-BHB was |
| doi_str_mv | 10.1080/10717544.2022.2036870 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_2638717864</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><doaj_id>oai_doaj_org_article_83ab728e25d8471185ce9c3e1c3981a2</doaj_id><sourcerecordid>2754996504</sourcerecordid><originalsourceid>FETCH-LOGICAL-c562t-bb556da89a35f199c0d3f7b7fad9046eaac64b3859a589dc6b9e472c1da27ac13</originalsourceid><addsrcrecordid>eNp9Uk1v1DAQjRCIlsJPAEXiwiXFH3Fsc0Cgio9KlbiUszWxJ7tenHixs0W588PxdrcV5YBk2db4zZsZv1dVLyk5p0SRt5RIKkXbnjPCWNl4pyR5VJ1SwWhD2q59XO4F0-xBJ9WznDeEEEWZeFqdcMGkJJqfVr-v11g7n228wbTUcah7TGX5CesSmNcp2mXGZo1jXIXY-6nOGIYGcsaxD0vtMPjb1LzkGcd3NdQTrgLaGV1tISWPqd5NDlNY_LSq_Zzr7RrSCDb-KFVmb_Pz6skAIeOL43lWff_86fria3P17cvlxcerxoqOzU3fC9E5UBq4GKjWljg-yF4O4HSZGAFs1_ZcCQ1CaWe7XmMrmaUOmARL-Vl1eeB1ETZmm_wIaTERvLkNxLQykEpDAY3i0EumkAmnWkmpEha15Ugt14oCK1zvD1zbXT-iszjNCcID0ocvk1-bVbwxShexpC4Eb44EKf7cYZ7NWGTAEGDCuMuGdVwViVXXFujrf6CbuEtT-SrDirxad4LsUeKAsinmnHC4b4YSs_eMufOM2XvGHD1T8l79Pcl91p1JCuDDAeCnIRbhfsUUnJlhCTENCSbrs-H_r_EHn5rUjQ</addsrcrecordid><sourcetype>Open Website</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2754996504</pqid></control><display><type>article</type><title>The discovery of berberine erythrocyte-hemoglobin self-assembly delivery system: a neglected carrier underlying its pharmacokinetics</title><source>Taylor & Francis Open Access</source><source>MEDLINE</source><source>DOAJ Directory of Open Access Journals</source><source>Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals</source><source>PubMed Central</source><source>Alma/SFX Local Collection</source><creator>Yu, Qiuxia ; Li, Minhua ; Chen, Hanbin ; Xu, Lieqiang ; Cheng, Juanjuan ; Lin, Guoshu ; Liu, Yuhong ; Su, Ziren ; Yang, Xiaobo ; Li, Yucui ; Chen, Jiannan ; Xie, Jianhui</creator><creatorcontrib>Yu, Qiuxia ; Li, Minhua ; Chen, Hanbin ; Xu, Lieqiang ; Cheng, Juanjuan ; Lin, Guoshu ; Liu, Yuhong ; Su, Ziren ; Yang, Xiaobo ; Li, Yucui ; Chen, Jiannan ; Xie, Jianhui</creatorcontrib><description>Berberine (BBR) has extremely low concentration and high tissue distribution. However, current pharmacokinetic studies predominantly focus on its concentration in plasma, which could hardly make a comprehensive understanding of its pharmacokinetic process. This study made a pioneering endeavor to explore the erythrocyte-hemoglobin (Hb) self-assembly system of BBR by exploring the interaction of BBR with erythrocyte and the combination of BBR with Hb. Results showed that BBR had a low bioavailability (C
0
= 2.833 μg/mL via intravenous administration of 2.5 mg/kg BBR and C
max
= 0.260 μg/mL via oral administration of 400 mg/kg BBR). Besides, BBR achieved higher concentrations in erythrocytes than plasma, and the erythrocytes count and Hb content were significantly decreased after intravenous administration. Hemolysis rate indicated the BBR-erythrocyte system (with 2% erythrocytes) was relatively stable without hemolysis at the concentration of 1.00 mg/mL. And the maximum percentage of drug loading was 100% when the BBR-erythrocyte concentration was 0.185 μg/mL. Furthermore, incubation of BBR and erythrocytes resulted in internalization of the erythrocyte membrane and the formation of intracellular vacuoles. The thermodynamic parameters indicated that the binding process of bovine hemoglobin (BHB) and BBR was spontaneous. UV-vis absorption spectra, synchronous fluorescence, circular dichroism and Raman spectra collectively indicated that BBR showed strong binding affinity toward BHB and affected the molecular environment of residues like tryptophan and tyrosine in BHB, resulting in the conformational changes of its secondary and tertiary structure. Molecular docking indicated BBR interacted with Arg-141 residue of BHB via hydrogen bond with the bond length of 2.55 Å. The ΔG value of the BHB-BBR system was −31.79 kJ/mol. Molecular dynamics simulation indicated the root mean square derivation of BBR-BHB was <0.025 nm, suggestive of stable conformation. Cumulatively, there was an erythrocyte-Hb self-assembled drug delivery system after oral or intravenous administration of BBR, which conceivably gained novel insight into the discrepancy between the extremely low plasma concentration and relatively high tissue concentration of BBR.</description><identifier>ISSN: 1071-7544</identifier><identifier>EISSN: 1521-0464</identifier><identifier>DOI: 10.1080/10717544.2022.2036870</identifier><identifier>PMID: 35277093</identifier><language>eng</language><publisher>England: Taylor & Francis</publisher><subject>Alzheimer's disease ; Berberine ; Berberine - chemistry ; Biological Availability ; Chinese medicine ; Drug delivery systems ; erythrocyte ; Erythrocytes ; Hemoglobin ; Hemoglobins - chemistry ; Hospitals ; Laboratory animals ; Medical research ; Molecular Docking Simulation ; Pharmaceutical sciences ; Pharmacokinetics ; Plasma ; self-assembly system</subject><ispartof>Drug delivery, 2022-12, Vol.29 (1), p.856-870</ispartof><rights>2022 The Author(s). Published by Informa UK Limited, trading as Taylor & Francis Group. 2022</rights><rights>2022 The Author(s). Published by Informa UK Limited, trading as Taylor & Francis Group. This work is licensed under the Creative Commons Attribution License http://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>2022 The Author(s). Published by Informa UK Limited, trading as Taylor & Francis Group. 2022 The Author(s)</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c562t-bb556da89a35f199c0d3f7b7fad9046eaac64b3859a589dc6b9e472c1da27ac13</citedby><cites>FETCH-LOGICAL-c562t-bb556da89a35f199c0d3f7b7fad9046eaac64b3859a589dc6b9e472c1da27ac13</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC8920379/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC8920379/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,860,881,2096,27479,27901,27902,53766,53768,59116,59117</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/35277093$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Yu, Qiuxia</creatorcontrib><creatorcontrib>Li, Minhua</creatorcontrib><creatorcontrib>Chen, Hanbin</creatorcontrib><creatorcontrib>Xu, Lieqiang</creatorcontrib><creatorcontrib>Cheng, Juanjuan</creatorcontrib><creatorcontrib>Lin, Guoshu</creatorcontrib><creatorcontrib>Liu, Yuhong</creatorcontrib><creatorcontrib>Su, Ziren</creatorcontrib><creatorcontrib>Yang, Xiaobo</creatorcontrib><creatorcontrib>Li, Yucui</creatorcontrib><creatorcontrib>Chen, Jiannan</creatorcontrib><creatorcontrib>Xie, Jianhui</creatorcontrib><title>The discovery of berberine erythrocyte-hemoglobin self-assembly delivery system: a neglected carrier underlying its pharmacokinetics</title><title>Drug delivery</title><addtitle>Drug Deliv</addtitle><description>Berberine (BBR) has extremely low concentration and high tissue distribution. However, current pharmacokinetic studies predominantly focus on its concentration in plasma, which could hardly make a comprehensive understanding of its pharmacokinetic process. This study made a pioneering endeavor to explore the erythrocyte-hemoglobin (Hb) self-assembly system of BBR by exploring the interaction of BBR with erythrocyte and the combination of BBR with Hb. Results showed that BBR had a low bioavailability (C
0
= 2.833 μg/mL via intravenous administration of 2.5 mg/kg BBR and C
max
= 0.260 μg/mL via oral administration of 400 mg/kg BBR). Besides, BBR achieved higher concentrations in erythrocytes than plasma, and the erythrocytes count and Hb content were significantly decreased after intravenous administration. Hemolysis rate indicated the BBR-erythrocyte system (with 2% erythrocytes) was relatively stable without hemolysis at the concentration of 1.00 mg/mL. And the maximum percentage of drug loading was 100% when the BBR-erythrocyte concentration was 0.185 μg/mL. Furthermore, incubation of BBR and erythrocytes resulted in internalization of the erythrocyte membrane and the formation of intracellular vacuoles. The thermodynamic parameters indicated that the binding process of bovine hemoglobin (BHB) and BBR was spontaneous. UV-vis absorption spectra, synchronous fluorescence, circular dichroism and Raman spectra collectively indicated that BBR showed strong binding affinity toward BHB and affected the molecular environment of residues like tryptophan and tyrosine in BHB, resulting in the conformational changes of its secondary and tertiary structure. Molecular docking indicated BBR interacted with Arg-141 residue of BHB via hydrogen bond with the bond length of 2.55 Å. The ΔG value of the BHB-BBR system was −31.79 kJ/mol. Molecular dynamics simulation indicated the root mean square derivation of BBR-BHB was <0.025 nm, suggestive of stable conformation. Cumulatively, there was an erythrocyte-Hb self-assembled drug delivery system after oral or intravenous administration of BBR, which conceivably gained novel insight into the discrepancy between the extremely low plasma concentration and relatively high tissue concentration of BBR.</description><subject>Alzheimer's disease</subject><subject>Berberine</subject><subject>Berberine - chemistry</subject><subject>Biological Availability</subject><subject>Chinese medicine</subject><subject>Drug delivery systems</subject><subject>erythrocyte</subject><subject>Erythrocytes</subject><subject>Hemoglobin</subject><subject>Hemoglobins - chemistry</subject><subject>Hospitals</subject><subject>Laboratory animals</subject><subject>Medical research</subject><subject>Molecular Docking Simulation</subject><subject>Pharmaceutical sciences</subject><subject>Pharmacokinetics</subject><subject>Plasma</subject><subject>self-assembly system</subject><issn>1071-7544</issn><issn>1521-0464</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2022</creationdate><recordtype>article</recordtype><sourceid>0YH</sourceid><sourceid>EIF</sourceid><sourceid>BENPR</sourceid><sourceid>DOA</sourceid><recordid>eNp9Uk1v1DAQjRCIlsJPAEXiwiXFH3Fsc0Cgio9KlbiUszWxJ7tenHixs0W588PxdrcV5YBk2db4zZsZv1dVLyk5p0SRt5RIKkXbnjPCWNl4pyR5VJ1SwWhD2q59XO4F0-xBJ9WznDeEEEWZeFqdcMGkJJqfVr-v11g7n228wbTUcah7TGX5CesSmNcp2mXGZo1jXIXY-6nOGIYGcsaxD0vtMPjb1LzkGcd3NdQTrgLaGV1tISWPqd5NDlNY_LSq_Zzr7RrSCDb-KFVmb_Pz6skAIeOL43lWff_86fria3P17cvlxcerxoqOzU3fC9E5UBq4GKjWljg-yF4O4HSZGAFs1_ZcCQ1CaWe7XmMrmaUOmARL-Vl1eeB1ETZmm_wIaTERvLkNxLQykEpDAY3i0EumkAmnWkmpEha15Ugt14oCK1zvD1zbXT-iszjNCcID0ocvk1-bVbwxShexpC4Eb44EKf7cYZ7NWGTAEGDCuMuGdVwViVXXFujrf6CbuEtT-SrDirxad4LsUeKAsinmnHC4b4YSs_eMufOM2XvGHD1T8l79Pcl91p1JCuDDAeCnIRbhfsUUnJlhCTENCSbrs-H_r_EHn5rUjQ</recordid><startdate>202212</startdate><enddate>202212</enddate><creator>Yu, Qiuxia</creator><creator>Li, Minhua</creator><creator>Chen, Hanbin</creator><creator>Xu, Lieqiang</creator><creator>Cheng, Juanjuan</creator><creator>Lin, Guoshu</creator><creator>Liu, Yuhong</creator><creator>Su, Ziren</creator><creator>Yang, Xiaobo</creator><creator>Li, Yucui</creator><creator>Chen, Jiannan</creator><creator>Xie, Jianhui</creator><general>Taylor & Francis</general><general>Taylor & Francis Ltd</general><general>Taylor & Francis Group</general><scope>0YH</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7X7</scope><scope>7XB</scope><scope>88I</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BENPR</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>M0S</scope><scope>M2P</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>Q9U</scope><scope>7X8</scope><scope>5PM</scope><scope>DOA</scope></search><sort><creationdate>202212</creationdate><title>The discovery of berberine erythrocyte-hemoglobin self-assembly delivery system: a neglected carrier underlying its pharmacokinetics</title><author>Yu, Qiuxia ; Li, Minhua ; Chen, Hanbin ; Xu, Lieqiang ; Cheng, Juanjuan ; Lin, Guoshu ; Liu, Yuhong ; Su, Ziren ; Yang, Xiaobo ; Li, Yucui ; Chen, Jiannan ; Xie, Jianhui</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c562t-bb556da89a35f199c0d3f7b7fad9046eaac64b3859a589dc6b9e472c1da27ac13</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2022</creationdate><topic>Alzheimer's disease</topic><topic>Berberine</topic><topic>Berberine - chemistry</topic><topic>Biological Availability</topic><topic>Chinese medicine</topic><topic>Drug delivery systems</topic><topic>erythrocyte</topic><topic>Erythrocytes</topic><topic>Hemoglobin</topic><topic>Hemoglobins - chemistry</topic><topic>Hospitals</topic><topic>Laboratory animals</topic><topic>Medical research</topic><topic>Molecular Docking Simulation</topic><topic>Pharmaceutical sciences</topic><topic>Pharmacokinetics</topic><topic>Plasma</topic><topic>self-assembly system</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Yu, Qiuxia</creatorcontrib><creatorcontrib>Li, Minhua</creatorcontrib><creatorcontrib>Chen, Hanbin</creatorcontrib><creatorcontrib>Xu, Lieqiang</creatorcontrib><creatorcontrib>Cheng, Juanjuan</creatorcontrib><creatorcontrib>Lin, Guoshu</creatorcontrib><creatorcontrib>Liu, Yuhong</creatorcontrib><creatorcontrib>Su, Ziren</creatorcontrib><creatorcontrib>Yang, Xiaobo</creatorcontrib><creatorcontrib>Li, Yucui</creatorcontrib><creatorcontrib>Chen, Jiannan</creatorcontrib><creatorcontrib>Xie, Jianhui</creatorcontrib><collection>Taylor & Francis Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Science Database (Alumni Edition)</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>ProQuest Central</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Science Database</collection><collection>Publicly Available Content Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>ProQuest Central Basic</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><collection>DOAJ Directory of Open Access Journals</collection><jtitle>Drug delivery</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Yu, Qiuxia</au><au>Li, Minhua</au><au>Chen, Hanbin</au><au>Xu, Lieqiang</au><au>Cheng, Juanjuan</au><au>Lin, Guoshu</au><au>Liu, Yuhong</au><au>Su, Ziren</au><au>Yang, Xiaobo</au><au>Li, Yucui</au><au>Chen, Jiannan</au><au>Xie, Jianhui</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The discovery of berberine erythrocyte-hemoglobin self-assembly delivery system: a neglected carrier underlying its pharmacokinetics</atitle><jtitle>Drug delivery</jtitle><addtitle>Drug Deliv</addtitle><date>2022-12</date><risdate>2022</risdate><volume>29</volume><issue>1</issue><spage>856</spage><epage>870</epage><pages>856-870</pages><issn>1071-7544</issn><eissn>1521-0464</eissn><abstract>Berberine (BBR) has extremely low concentration and high tissue distribution. However, current pharmacokinetic studies predominantly focus on its concentration in plasma, which could hardly make a comprehensive understanding of its pharmacokinetic process. This study made a pioneering endeavor to explore the erythrocyte-hemoglobin (Hb) self-assembly system of BBR by exploring the interaction of BBR with erythrocyte and the combination of BBR with Hb. Results showed that BBR had a low bioavailability (C
0
= 2.833 μg/mL via intravenous administration of 2.5 mg/kg BBR and C
max
= 0.260 μg/mL via oral administration of 400 mg/kg BBR). Besides, BBR achieved higher concentrations in erythrocytes than plasma, and the erythrocytes count and Hb content were significantly decreased after intravenous administration. Hemolysis rate indicated the BBR-erythrocyte system (with 2% erythrocytes) was relatively stable without hemolysis at the concentration of 1.00 mg/mL. And the maximum percentage of drug loading was 100% when the BBR-erythrocyte concentration was 0.185 μg/mL. Furthermore, incubation of BBR and erythrocytes resulted in internalization of the erythrocyte membrane and the formation of intracellular vacuoles. The thermodynamic parameters indicated that the binding process of bovine hemoglobin (BHB) and BBR was spontaneous. UV-vis absorption spectra, synchronous fluorescence, circular dichroism and Raman spectra collectively indicated that BBR showed strong binding affinity toward BHB and affected the molecular environment of residues like tryptophan and tyrosine in BHB, resulting in the conformational changes of its secondary and tertiary structure. Molecular docking indicated BBR interacted with Arg-141 residue of BHB via hydrogen bond with the bond length of 2.55 Å. The ΔG value of the BHB-BBR system was −31.79 kJ/mol. Molecular dynamics simulation indicated the root mean square derivation of BBR-BHB was <0.025 nm, suggestive of stable conformation. Cumulatively, there was an erythrocyte-Hb self-assembled drug delivery system after oral or intravenous administration of BBR, which conceivably gained novel insight into the discrepancy between the extremely low plasma concentration and relatively high tissue concentration of BBR.</abstract><cop>England</cop><pub>Taylor & Francis</pub><pmid>35277093</pmid><doi>10.1080/10717544.2022.2036870</doi><tpages>15</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Alzheimer's disease Berberine Berberine - chemistry Biological Availability Chinese medicine Drug delivery systems erythrocyte Erythrocytes Hemoglobin Hemoglobins - chemistry Hospitals Laboratory animals Medical research Molecular Docking Simulation Pharmaceutical sciences Pharmacokinetics Plasma self-assembly system |
| title | The discovery of berberine erythrocyte-hemoglobin self-assembly delivery system: a neglected carrier underlying its pharmacokinetics |
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