Gram-negative bacterial cells are surrounded by a cell membrane which protects the cell and controls the transport of nutrients and waste products in and out of the cells at a fast rate. This rapid transport of nutrients and wastes through the cell membrane is made possible by channel proteins called porins. Various types of porins present in the cell membrane have specific functions depending on their selectivity towards different nutrients, and channel proteins selective towards water are called aquaporins. These proteins restrict the passage of all entities except water molecules and they provide a fast transport rate of water molecules at 109 molecules/second per channel. The high selectivity of porins has led to their incorporation into synthetic systems, and one example is the addition of porins to separations membranes in order to enhance their performance in terms of selectivity and permeability, in a field called biomimetics. The concept of incorporating aquaporins into synthetic membranes has been studied for the last 10 years in order to enhance the water permeability and selectivity of membranes for water purification; however, there are still limitations such as high costs, difficulties in fabrication of aquaporins, their alignment into synthetic membrane assembly, low stability, and limitations on number of aquaporin molecules that can be introduced into synthetic membranes limit their applicability. In recent years, concurrent with the work on aquaporin-based biomimetic membranes, there has been an increase in the study of synthesizing molecules with similar structure-function relationships of aquaporins. These artificial channels attempt to mimic the high-water permeability and selectivity of aquaporins, while being synthesized using simple chemistry, being solvent compatible, and requiring less space on the membrane surface which helps to incorporate more channels into the membrane assembly. The objectives of this study were to first incorporate aquaporins into synthetic nanofiltration membranes without chemical alteration them to prevent flattening or denaturing of aquaporins; then, the second objective was to install functional groups on aquaporins and align them in the direction of water flow; lastly, the third objective was to synthesize artificial channels in order to overcome the issues with aquaporin stability, alignment, and efficient packing of water channels onto the membrane surface. For the first objective, aquaporins were treated with a polysaccharide, gum Arabic, and incorporated into an amphiphilic polymer, polyvinyl alcohol with alkyl side chains (PVA-alkyl), in order to simulate the natural housing of lipid bilayer for aquaporins and to protect them from denaturing. Long alkyl chains provided the hydrophobic component, while PVA provided the hydrophilic component of the amphiphilic polymer. Membranes modified with aquaporins displayed lower flux declines and higher flux recoveries after reverse flow filtration, along with improved rejection values for both protein and salt solutions as compared to PBI and PBI-PVA-alkyl membranes. However, there was leakage of ions between channels. Therefore, in order to improve the rejection of protons, ions and other impurities, the channels were aligned with the direction of water flow. Functional groups were installed on Aquaporins using site-directed mutagenesis for covalent attachment to the polymer matrix so that the proteins could be immobilized to the membranes and aligned in the direction of the flow. Aquaporin constructs were modified to bear affinity tags or unique amino acids at the N-terminus of the aquaporin molecule, which was used to facilitate directional immobilization. Each aquaporin monomer was modified with a unique amino acid Cys group at the N-terminus right after the first Met, and due to the aquaporin tetrameric nature, these Cys groups became four anchors for attachment. The presence of these four Cys anchors per aquaporin tetramer was used to attach on the membrane surface in alignment with the feed water flow direction. Membranes modified with mutated aquaporins showed consistently higher salt rejection values of ~70% irrespective of feed concentration, along with higher flux recoveries and lower flux declines. Commercial NF-270 membranes provide a monovalent salt (NaCl) rejection of ~50% and divalent salt (MgCl2) rejection of 97%. Also, approximate coverage of membrane surface with attached aquaporins was calculated using simulation studies. Simulation studies showed that immobilized aquaporins with PVA-alkyl provided a diffusion rate equivalent to 64% coverage on the membrane surface. This showed that aquaporins didn’t cover the entire surface area of the membrane. However, immobilized aquaporins were responsible for the rejection of a portion of ions passing through the membrane. In order to overcome the limitations of aquaporin incorporation into polymer membranes, artificial organic frameworks were added as surface modification on PBI membranes. Organic frameworks were synthesized as derivatives of hybrid bisamides. The series of bisamides 1-4 consist of 6-amino-pyridine-2-dicarboxylic acid, 6-hydroxymethyl-pyridine-2-carboxylic acid and ethylenediamine, trimethylenediamine, putrescine, and cadaverine depending on the length of carbon chain. These frameworks are amphiphilic in nature and have strong chemical attachment due to the presence of amines and carboxylic acids into each building block. These molecules were introduced into the membrane matrix using carbodiimide chemistry. FTIR results showed the attachment of these bisamide molecules onto the surface of a modified PBI membrane. Also, modified membranes showed a reduced molecular weight cut off (MWCO) for neutral organic molecules. Overall, membranes modified with aquaporins have shown a potential to provide consistently high salt rejections with increasing feed solutions. Also, preliminary results have shown that bisamide molecules can be attached onto the membrane surface as organic frameworks and have a potential to be an alternative for aquaporins based biomimetic membranes.