{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,8]],"date-time":"2026-02-08T02:34:44Z","timestamp":1770518084289,"version":"3.49.0"},"reference-count":20,"publisher":"MDPI AG","issue":"8","license":[{"start":{"date-parts":[[2021,4,14]],"date-time":"2021-04-14T00:00:00Z","timestamp":1618358400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Sensors"],"abstract":"<jats:p>This perspective presents an overview of approaches to the preparation of molecular recognition agents for chemical sensing. These approaches include chemical synthesis, using catalysts from biological systems, partitioning, aptamers, antibodies and molecularly imprinted polymers. The latter three approaches are general in that they can be applied with a large number of analytes, both proteins and smaller molecules like drugs and hormones. Aptamers and antibodies bind analytes rapidly while molecularly imprinted polymers bind much more slowly. Most molecularly imprinted polymers, formed by polymerizing in the presence of a template, contain a high level of covalent crosslinker that causes the polymer to form a separate phase. This results in a material that is rigid with low affinity for analyte and slow binding kinetics. Our approach to templating is to use predominantly or exclusively noncovalent crosslinks. This results in soluble templated polymers that bind analyte rapidly with high affinity. The biggest challenge of this approach is that the chains are tangled when the templated polymer is dissolved in water, blocking access to binding sites.<\/jats:p>","DOI":"10.3390\/s21082757","type":"journal-article","created":{"date-parts":[[2021,4,14]],"date-time":"2021-04-14T04:21:08Z","timestamp":1618374068000},"page":"2757","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":9,"title":["Molecular Recognition: Perspective and a New Approach"],"prefix":"10.3390","volume":"21","author":[{"given":"W. Rudolf","family":"Seitz","sequence":"first","affiliation":[{"name":"Department of Chemistry, University of New Hampshire, Durham, NH 03824, USA"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-5370-8286","authenticated-orcid":false,"given":"Casey J.","family":"Grenier","sequence":"additional","affiliation":[{"name":"Tekscan, Inc., 307 W. First St., Boston, MA 02127, USA"}]},{"given":"John R.","family":"Csoros","sequence":"additional","affiliation":[{"name":"Department of Chemistry, University of New Hampshire, Durham, NH 03824, USA"}]},{"given":"Rongfang","family":"Yang","sequence":"additional","affiliation":[{"name":"Community College of Rhode Island, 400 East Ave., Warwick, RI 02886, USA"}]},{"given":"Tianyu","family":"Ren","sequence":"additional","affiliation":[{"name":"Department of Chemistry, University of New Hampshire, Durham, NH 03824, USA"}]}],"member":"1968","published-online":{"date-parts":[[2021,4,14]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","unstructured":"Grenier, C.J., Timberman, A., Yang, R., Csoros, J., Papantones, A., Deravi, L., and Seitz, W.R. (2018). Rapid, High Affinity Binding by a Fluorescein Templated Copolymer Combining Covalent, Hydrophobic and Acid-Base Noncovalent Crosslinks. 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USA"},{"key":"ref_12","doi-asserted-by":"crossref","unstructured":"Elskens, J.R., Elskens, J.M., and Madder, A. (2020). Chemical Modification of Aptamers for Increased Binding Affinity in Diagnostic Applications: Current Status and Future Prospects. Int. J. Mol. Sci., 21.","DOI":"10.3390\/ijms21124522"},{"key":"ref_13","doi-asserted-by":"crossref","unstructured":"Somerson, J., and Plaxco, K.W. (2018). Electrochemical Aptamer-based Sensors for Rapid Point-of-use Monitoring of the Mycotoxin Ochratoxin A directly in a food stream. Molecules, 23.","DOI":"10.3390\/molecules23040912"},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"86","DOI":"10.1016\/j.jim.2014.12.011","article-title":"Measuring Affinity Constants of 1450 Monoclonal Antibodies to Peptide Targets with a Microarray-based Label-Free Assay Platform","volume":"417","author":"Landry","year":"2005","journal-title":"J. Immunol. 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